The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome.
The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.
Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
A transfer RNA which is specific for carrying glycine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.
A group of transfer RNAs which are specific for carrying each one of the 20 amino acids to the ribosome in preparation for protein synthesis.
A transfer RNA which is specific for carrying lysine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying tryptophan to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying arginine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying isoleucine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying methionine to sites on the ribosomes. During initiation of protein synthesis, tRNA(f)Met in prokaryotic cells and tRNA(i)Met in eukaryotic cells binds to the start codon (CODON, INITIATOR).
A transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10.
A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).
A transfer RNA which is specific for carrying tyrosine to sites on the ribosomes in preparation for protein synthesis.
A modified nucleoside which is present in the first position of the anticodon of tRNA-tyrosine, tRNA-histidine, tRNA-asparagine and tRNA-aspartic acid of many organisms. It is believed to play a role in the regulatory function of tRNA. Nucleoside Q can be further modified to nucleoside Q*, which has a mannose or galactose moiety linked to position 4 of its cyclopentenediol moiety.
A transfer RNA which is specific for carrying aspartic acid to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying glutamic acid to sites on the ribosomes in preparation for protein synthesis.
Pseudouridine is a modified nucleoside, where the uracil component of a uridine residue in RNA molecules is linked to ribose through a carbon-carbon bond rather than the usual nitrogen-glycosidic bond, which can contribute to structural stability and functional diversity in RNA.
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
A transfer RNA which is specific for carrying proline to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying cysteine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying leucine to sites on the ribosomes in preparation for protein synthesis.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Mutation process that restores the wild-type PHENOTYPE in an organism possessing a mutationally altered GENOTYPE. The second "suppressor" mutation may be on a different gene, on the same gene but located at a distance from the site of the primary mutation, or in extrachromosomal genes (EXTRACHROMOSOMAL INHERITANCE).
A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.
The conversion of uncharged TRANSFER RNA to AMINO ACYL TRNA.
A transfer RNA which is specific for carrying alanine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying valine to sites on the ribosomes in preparation for protein synthesis.
N(6)-[delta(3)-isopentenyl]adenosine. Isopentenyl derivative of adenosine which is a member of the cytokinin family of plant growth regulators.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The meaning ascribed to the BASE SEQUENCE with respect to how it is translated into AMINO ACID SEQUENCE. The start, stop, and order of amino acids of a protein is specified by consecutive triplets of nucleotides called codons (CODON).
A photoactivable URIDINE analog that is used as an affinity label.
Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.
Uridine is a nucleoside, specifically a derivative of pyrimidine, that is composed of a uracil molecule joined to a ribose sugar molecule through a β-N1 glycosidic bond, and has significant roles in RNA synthesis, energy transfer, and cell signaling.
A transfer RNA which is specific for carrying histidine to sites on the ribosomes in preparation for protein synthesis.
A group of ribonucleotides (up to 12) in which the phosphate residues of each ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
A reaction that introduces an aminoacyl group to a molecule. TRANSFER RNA AMINOACYLATION is the first step in GENETIC TRANSLATION.
Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.
Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.
An enzyme that activates lysine with its specific transfer RNA. EC 6.1.1.6.
Pairing of purine and pyrimidine bases by HYDROGEN BONDING in double-stranded DNA or RNA.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Ribonucleic acid in fungi having regulatory and catalytic roles as well as involvement in protein synthesis.
An enzyme that activates glycine with its specific transfer RNA. EC 6.1.1.14.
A pyrimidine nucleoside that is composed of the base CYTOSINE linked to the five-carbon sugar D-RIBOSE.
The addition of an organic acid radical into a molecule.
An enzyme that activates threonine with its specific transfer RNA. EC 6.1.1.3.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-.
A directed change in translational READING FRAMES that allows the production of a single protein from two or more OVERLAPPING GENES. The process is programmed by the nucleotide sequence of the MRNA and is sometimes also affected by the secondary or tertiary mRNA structure. It has been described mainly in VIRUSES (especially RETROVIRUSES); RETROTRANSPOSONS; and bacterial insertion elements but also in some cellular genes.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A purine nucleoside that has guanine linked by its N9 nitrogen to the C1 carbon of ribose. It is a component of ribonucleic acid and its nucleotides play important roles in metabolism. (From Dorland, 28th ed)
An enzyme catalyzing the endonucleolytic cleavage of RNA at the 3'-position of a guanylate residue. EC 3.1.27.3.
An enzyme that activates tryptophan with its specific transfer RNA. EC 6.1.1.2.
An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.
An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12.
Any codon that signals the termination of genetic translation (TRANSLATION, GENETIC). PEPTIDE TERMINATION FACTORS bind to the stop codon and trigger the hydrolysis of the aminoacyl bond connecting the completed polypeptide to the tRNA. Terminator codons do not specify amino acids.
Post-transcriptional biological modification of messenger, transfer, or ribosomal RNAs or their precursors. It includes cleavage, methylation, thiolation, isopentenylation, pseudouridine formation, conformational changes, and association with ribosomal protein.
The relative amounts of the PURINES and PYRIMIDINES in a nucleic acid.
An enzyme that activates valine with its specific transfer RNA. EC 6.1.1.9
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
An enzyme that activates tyrosine with its specific transfer RNA. EC 6.1.1.1.
A transfer RNA which is specific for carrying asparagine to sites on the ribosomes in preparation for protein synthesis.
An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19.
An enzyme that catalyzes the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyzes the covalent joining of two polyribonucleotides in phosphodiester linkage. EC 6.5.1.3.
An enzyme that activates phenylalanine with its specific transfer RNA. EC 6.1.1.20.
An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.
An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.

Single atom modification (O-->S) of tRNA confers ribosome binding. (1/763)

Escherichia coli tRNALysSUU, as well as human tRNALys3SUU, has 2-thiouridine derivatives at wobble position 34 (s2U*34). Unlike the native tRNALysSUU, the full-length, unmodified transcript of human tRNALys3UUU and the unmodified tRNALys3UUU anticodon stem/loop (ASLLys3UUU) did not bind AAA- or AAG-programmed ribosomes. In contrast, the completely unmodified yeast tRNAPhe anticodon stem/loop (ASLPheGAA) had an affinity (Kd = 136+/-49 nM) similar to that of native yeast tRNAPheGmAA (Kd = 103+/-19 nM). We have found that the single, site-specific substitution of s2U34 for U34 to produce the modified ASLLysSUU was sufficient to restore ribosomal binding. The modified ASLLysSUU bound the ribosome with an affinity (Kd = 176+/-62 nM) comparable to that of native tRNALysSUU (Kd = 70+/-7 nM). Furthermore, in binding to the ribosome, the modified ASLLys3SUU produced the same 16S P-site tRNA footprint as did native E. coli tRNALysSUU, yeast tRNAPheGmAA, and the unmodified ASLPheGAA. The unmodified ASLLys3UUU had no footprint at all. Investigations of thermal stability and structure monitored by UV spectroscopy and NMR showed that the dynamic conformation of the loop of modified ASLLys3SUU was different from that of the unmodified ASLLysUUU, whereas the stems were isomorphous. Based on these and other data, we conclude that s2U34 in tRNALysSUU and in other s2U34-containing tRNAs is critical for generating an anticodon conformation that leads to effective codon interaction in all organisms. This is the first example of a single atom substitution (U34-->s2U34) that confers the property of ribosomal binding on an otherwise inactive tRNA.  (+info)

The presence of pseudouridine in the anticodon alters the genetic code: a possible mechanism for assignment of the AAA lysine codon as asparagine in echinoderm mitochondria. (2/763)

It has been inferred from DNA sequence analyses that in echinoderm mitochondria not only the usual asparagine codons AAU and AAC, but also the usual lysine codon AAA, are translated as asparagine by a single mitochondrial (mt) tRNAAsn with the anticodon GUU. Nucleotide sequencing of starfish mt tRNAAsn revealed that the anticodon is GPsiU, U35 at the anticodon second position being modified to pseudouridine (Psi). In contrast, mt tRNALys, corresponding to another lysine codon, AAG, has the anticodon CUU. mt tRNAs possessing anti-codons closely related to that of tRNAAsn, but responsible for decoding only two codons each-tRNAHis, tRNAAsp and tRNATyr-were found to possess unmodified U35 in all cases, suggesting the importance of Psi35 for decoding the three codons. Therefore, the decoding capabilities of two synthetic Escherichia coli tRNAAla variants with the anticodon GPsiU or GUU were examined using an E.coli in vitro translation system. Both tRNAs could translate not only AAC and AAU with similar efficiency, but also AAA with an efficiency that was approximately 2-fold higher in the case of tRNAAlaGPsiU than tRNAAlaGUU. These findings imply that Psi35 of echinoderm mt tRNAAsn actually serves to decode the unusual asparagine codon AAA, resulting in the alteration of the genetic code in echinoderm mitochondria.  (+info)

A cytotoxic ribonuclease targeting specific transfer RNA anticodons. (3/763)

The carboxyl-terminal domain of colicin E5 was shown to inhibit protein synthesis of Escherichia coli. Its target, as revealed through in vivo and in vitro experiments, was not ribosomes as in the case of E3, but the transfer RNAs (tRNAs) for Tyr, His, Asn, and Asp, which contain a modified base, queuine, at the wobble position of each anticodon. The E5 carboxyl-terminal domain hydrolyzed these tRNAs just on the 3' side of this nucleotide. Tight correlation was observed between the toxicity of E5 and the cleavage of intracellular tRNAs of this group, implying that these tRNAs are the primary targets of colicin E5.  (+info)

Secondary structure of the C-terminal domain of the tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus: a novel type of anticodon binding domain? (4/763)

The tyrosyl-tRNA synthetase catalyzes the activation of tyrosine and its coupling to the cognate tRNA. The enzyme is made of two domains: an N-terminal catalytic domain and a C-terminal domain that is necessary for tRNA binding and for which it was not possible to determine the structure by X-ray crystallography. We determined the secondary structure of the C-terminal domain of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus by nuclear magnetic resonance methods and found that it is of the alpha+beta type. Its arrangement differs from those of the other anticodon binding domains whose structure is known. We also found that the isolated C-terminal domain behaves as a folded globular protein, and we suggest the presence of a flexible linker between the two domains.  (+info)

Differential import of nuclear-encoded tRNAGly isoacceptors into solanum Tuberosum mitochondria. (5/763)

In potato ( Solanum tuberosum ) mitochondria, about two-thirds of the tRNAs are encoded by the mitochondrial genome and one-third is imported from the cytosol. In the case of tRNAGly isoacceptors, a mitochondrial-encoded tRNAGly(GCC) was found in potato mitochondria, but this is likely to be insufficient to decode the four GGN glycine codons. In this work, we identified a cytosolic tRNAGly(UCC), which was found to be present in S.tuberosum mitochondria. The cytosolic tRNAGly(CCC) was also present in mitochondria, but to a lesser extent. By contrast, the cytosolic tRNAGly(GCC) could not be detected in mitochondria. This selective import of tRNAGly isoacceptors into S. tuberosum mitochondria raises further questions about the mechanism under-lying the specificity of the import process.  (+info)

The peculiar architectural framework of tRNASec is fully recognized by yeast AspRS. (6/763)

The wild-type transcript of Escherichia coli tRNASec, characterized by a peculiar core architecture and a large variable region, was shown to be aspartylatable by yeast AspRS. Similar activities were found for tRNASec mutants with methionine, leucine, and tryptophan anticodons. The charging efficiency of these molecules was found comparable to that of a minihelix derived from tRNAAsp and is accounted for by the presence of the discriminator residue G73, which is a major aspartate identity determinant. Introducing the aspartate identity elements from the anticodon loop (G34, U35, C36, C38) into tRNASec transforms this molecule into an aspartate acceptor with kinetic properties identical to tRNAAsp. Expression of the aspartate identity set in tRNASec is independent of the size of its variable region. The functional study was completed by footprinting experiments with four different nucleases as structural probes. Protection patterns by AspRS of transplanted tRNASec and tRNAAsp were found similar. They are modified, particularly in the anticodon loop, upon changing the aspartate anticodon into that of methionine. Altogether, it appears that recognition of a tRNA by AspRS is more governed by the presence of the aspartate identity set than by the structural framework that carries this set.  (+info)

The uridine in "U-turn": contributions to tRNA-ribosomal binding. (7/763)

"U-turns" represent an important class of structural motifs in the RNA world, wherein a uridine is involved in an abrupt change in the direction of the polynucleotide backbone. In the crystal structure of yeast tRNAPhe, the invariant uridine at position 33 (U33), adjacent to the anticodon, stabilizes the exemplar U-turn with three non-Watson-Crick interactions: hydrogen bonding of the 2'-OH to N7 of A35 and the N3-H to A36-phosphate, and stacking between C32 and A35-phosphate. The functional importance of each noncanonical interaction was determined by assaying the ribosomal binding affinities of tRNAPhe anticodon stem and loop domains (ASLs) with substitutions at U33. An unsubstituted ASL bound 30S ribosomal subunits with an affinity (Kd = 140+/-50 nM) comparable to that of native yeast tRNAPhe (Kd = 100+/-20 nM). However, the binding affinities of ASLs with dU-33 (no 2'-OH) and C-33 (no N3-H) were significantly reduced (2,930+/-140 nM and 2,190+/-300 nM, respectively). Surprisingly, the ASL with N3-methyluridine-33 (no N3-H) bound ribosomes with a high affinity (Kd = 220+/-20 nM). In contrast, ASLs constructed with position 33 uridine analogs in nonstacking, nonnative, and constrained conformations, dihydrouridine (C2'-endo), 6-methyluridine (syn) and 2'O-methyluridine (C3'-endo) had almost undetectable binding. The inability of ASLs with 6-methyluridine-33 and 2'O-methyluridine-33 to bind ribosomes was not attributable to any thermal instability of the RNAs. These results demonstrate that proton donations by the N3-H and 2'OH groups of U33 are not absolutely required for ribosomal binding. Rather, the results suggest that the overall uridine conformation, including a dynamic (C3'-endo > C2'-endo) sugar pucker, anti conformation, and ability of uracil to stack between C32 and A35-phosphate, are the contributing factors to a functional U-turn.  (+info)

A single uridine modification at the wobble position of an artificial tRNA enhances wobbling in an Escherichia coli cell-free translation system. (8/763)

5-Methoxyuridine was introduced into the first position of the anticodon of the unmodified form of tRNA(1Ser) from Escherichia coli. The codon reading efficiencies of this tRNA (tRNA(5-methoxyuridine UGA)) relative to those of the unmodified counterpart (tRNA(UGA)) were measured in a cell-free translation system. tRNA(5-methoxyuridine UGA) was more efficient than tRNA(UGA) in the reading of the UCU and UCG codons and was less efficient in the reading of the UCA codon. Thus, the single modification of U to 5-methoxyuridine can enhance the wobble readings.  (+info)

An anticodon is a sequence of three ribonucleotides (RNA bases) in a transfer RNA (tRNA) molecule that pair with a complementary codon in a messenger RNA (mRNA) molecule during protein synthesis. This interaction occurs within the ribosome during translation, where the genetic code in the mRNA is translated into an amino acid sequence in a polypeptide. Specifically, each tRNA carries a specific amino acid that corresponds to its anticodon sequence, allowing for the accurate and systematic addition of amino acids to the growing polypeptide chain.

In summary, an anticodon is a crucial component of the translation machinery, facilitating the precise decoding of genetic information and enabling the synthesis of proteins according to the instructions encoded in mRNA molecules.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis, the process by which cells create proteins. In protein synthesis, tRNAs serve as adaptors, translating the genetic code present in messenger RNA (mRNA) into the corresponding amino acids required to build a protein.

Each tRNA molecule has a distinct structure, consisting of approximately 70-90 nucleotides arranged in a cloverleaf shape with several loops and stems. The most important feature of a tRNA is its anticodon, a sequence of three nucleotides located in one of the loops. This anticodon base-pairs with a complementary codon on the mRNA during translation, ensuring that the correct amino acid is added to the growing polypeptide chain.

Before tRNAs can participate in protein synthesis, they must be charged with their specific amino acids through an enzymatic process involving aminoacyl-tRNA synthetases. These enzymes recognize and bind to both the tRNA and its corresponding amino acid, forming a covalent bond between them. Once charged, the aminoacyl-tRNA complex is ready to engage in translation and contribute to protein formation.

In summary, transfer RNA (tRNA) is a small RNA molecule that facilitates protein synthesis by translating genetic information from messenger RNA into specific amino acids, ultimately leading to the creation of functional proteins within cells.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis. It serves as the adaptor molecule that translates the genetic code present in messenger RNA (mRNA) into the corresponding amino acids, which are then linked together to form a polypeptide chain during protein synthesis.

Aminoacyl tRNA is a specific type of tRNA molecule that has been charged or activated with an amino acid. This process is called aminoacylation and is carried out by enzymes called aminoacyl-tRNA synthetases. Each synthetase specifically recognizes and attaches a particular amino acid to its corresponding tRNA, ensuring the fidelity of protein synthesis. Once an amino acid is attached to a tRNA, it forms an aminoacyl-tRNA complex, which can then participate in translation and contribute to the formation of a new protein.

Nucleic acid conformation refers to the three-dimensional structure that nucleic acids (DNA and RNA) adopt as a result of the bonding patterns between the atoms within the molecule. The primary structure of nucleic acids is determined by the sequence of nucleotides, while the conformation is influenced by factors such as the sugar-phosphate backbone, base stacking, and hydrogen bonding.

Two common conformations of DNA are the B-form and the A-form. The B-form is a right-handed helix with a diameter of about 20 Å and a pitch of 34 Å, while the A-form has a smaller diameter (about 18 Å) and a shorter pitch (about 25 Å). RNA typically adopts an A-form conformation.

The conformation of nucleic acids can have significant implications for their function, as it can affect their ability to interact with other molecules such as proteins or drugs. Understanding the conformational properties of nucleic acids is therefore an important area of research in molecular biology and medicine.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis. During this process, tRNAs serve as adaptors between the mRNA (messenger RNA) molecules and the amino acids used to construct proteins. Each tRNA contains a specific anticodon sequence that can base-pair with a complementary codon on the mRNA. At the other end of the tRNA, there is a site where an amino acid can attach. This attachment is facilitated by enzymes called aminoacyl tRNA synthetases, which recognize specific tRNAs and catalyze the formation of the ester bond between the tRNA and its cognate amino acid.

Gly (glycine) is one of the 20 standard amino acids found in proteins. It has a simple structure, consisting of an amino group (-NH2), a carboxylic acid group (-COOH), a hydrogen atom (-H), and a side chain made up of a single hydrogen atom (-CH2-). Glycine is the smallest and most flexible of all amino acids due to its lack of a bulky side chain, which allows it to fit into tight spaces within protein structures.

Therefore, 'RNA, Transfer, Gly' can be understood as a transfer RNA (tRNA) molecule specifically responsible for delivering the amino acid glycine (-Gly) during protein synthesis. This tRNA will have an anticodon sequence that base-pairs with the mRNA codons specifying glycine: GGU, GGC, GGA, or GGG.

Transfer RNA (tRNA) is a type of RNA molecule that helps translate genetic information from messenger RNA (mRNA) into proteins. Each tRNA carries a specific amino acid to the growing polypeptide chain during protein synthesis, based on the anticodon sequence in its variable loop region that recognizes and binds to a complementary codon sequence in the mRNA.

Phenylalanine (Phe) is one of the twenty standard amino acids found in proteins. It has a hydrophobic side chain, which means it tends to repel water and interact with other non-polar molecules. In tRNA, phenylalanine is attached to a specific tRNA molecule known as tRNAPhe. This tRNA recognizes the mRNA codons UUC and UUU, which specify phenylalanine during protein synthesis.

Transfer RNA (tRNA) are small RNA molecules that play a crucial role in protein synthesis. They are responsible for translating the genetic code contained within messenger RNA (mRNA) into the specific sequence of amino acids during protein synthesis.

Amino acid-specific tRNAs are specialized tRNAs that recognize and bind to specific amino acids. Each tRNA has an anticodon region that can base-pair with a complementary codon on the mRNA, which determines the specific amino acid that will be added to the growing polypeptide chain during protein synthesis.

Therefore, a more detailed medical definition of "RNA, Transfer, Amino Acid-Specific" would be:

A type of transfer RNA (tRNA) molecule that is specific to a particular amino acid and plays a role in translating the genetic code contained within messenger RNA (mRNA) into the specific sequence of amino acids during protein synthesis. The anticodon region of an amino acid-specific tRNA base-pairs with a complementary codon on the mRNA, which determines the specific amino acid that will be added to the growing polypeptide chain during protein synthesis.

I'm happy to help! Here are the definitions for each of those terms:

1. RNA (Ribonucleic Acid): RNA is a nucleic acid that plays a crucial role in the process of gene expression. It carries genetic information from DNA to the ribosomes, where proteins are synthesized. RNA is made up of a long chain of nucleotides, just like DNA, but with some key differences in its structure and composition.
2. Transfer: In the context of biochemistry, "transfer" refers to the movement or transport of molecules from one location to another within a cell or between cells. This process is often facilitated by specific proteins or other molecular carriers.
3. Lys (Lysine): Lysine is an essential amino acid that cannot be synthesized by the human body and must be obtained through diet. It plays important roles in various biological processes, including protein synthesis, enzyme function, hormone production, and energy metabolism. In molecular biology, lysine is often used as a marker for certain types of modifications to proteins or nucleic acids.

Therefore, "RNA, Transfer, Lys" could refer to the transfer RNA (tRNA) molecule that carries a specific amino acid, such as lysine, to the ribosome during protein synthesis. The tRNA molecule recognizes a specific codon on the messenger RNA (mRNA) and brings the corresponding amino acid to the growing polypeptide chain, allowing for the translation of genetic information into a functional protein.

Transfer RNA (tRNA) for tryptophan (Trp) is a specific type of tRNA molecule that plays a crucial role in protein synthesis. In the process of translation, genetic information from messenger RNA (mRNA) is translated into a corresponding sequence of amino acids to form a protein.

Tryptophan is one of the twenty standard amino acids found in proteins. Each tRNA molecule carries a specific amino acid that corresponds to a particular codon (a sequence of three nucleotides) on the mRNA. The tRNA with tryptophan attached to it recognizes and binds to the mRNA codon UGG, which is the only codon that specifies tryptophan in the genetic code.

The tRNA molecule has a characteristic cloverleaf-like structure, composed of a stem region made up of base pairs and loop regions containing unpaired nucleotides. The anticodon loop contains the complementary sequence to the mRNA codon, allowing for specific recognition and binding. The other end of the tRNA molecule carries the amino acid, in this case tryptophan, which is attached via an ester linkage to a specific nucleotide called the 3'-end of the tRNA.

In summary, tRNA (Trp) is a key player in protein synthesis, responsible for delivering tryptophan to the ribosome during translation, where it can be incorporated into the growing polypeptide chain according to the genetic information encoded in mRNA.

I'm happy to help! However, it seems like the term you're looking for is "Transfer RNA arginine," not "Arg." Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis. Specifically, tRNAs are responsible for delivering amino acids to the ribosome, where they are joined together to form proteins.

Each tRNA molecule contains a specific anticodon sequence that can base-pair with a complementary codon sequence on messenger RNA (mRNA). When a tRNA molecule encounters an mRNA codon that matches its anticodon, it binds to the mRNA and delivers the amino acid associated with that tRNA.

In the case of tRNA arginine, this type of tRNA is responsible for delivering the amino acid arginine to the ribosome during protein synthesis. Arginine is a positively charged amino acid that plays important roles in various cellular processes, including protein structure and function, signal transduction, and gene regulation.

Therefore, Transfer RNA arginine refers to the specific tRNA molecule that delivers the amino acid arginine during protein synthesis.

Transfer RNA (tRNA) that carries the amino acid isoleucine is referred to as 'tRNA-Ile' in medical and molecular biology terminology.

tRNAs are specialized RNA molecules that play a crucial role in protein synthesis, by transporting specific amino acids from the cytoplasm to the ribosomes, where proteins are assembled. Each tRNA has an anticodon region that recognizes and binds to a complementary codon sequence on messenger RNA (mRNA). When a tRNA with the correct anticodon pairs with an mRNA codon during translation, the attached amino acid is added to the growing polypeptide chain.

Ile, or isoleucine, is a genetically encoded, hydrophobic amino acid that is one of the 20 standard amino acids found in proteins. Isoleucine is transported by its specific tRNA-Ile molecule during protein synthesis.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis, the process by which cells create proteins. During protein synthesis, tRNAs serve as adaptors, translating the genetic code present in messenger RNA (mRNA) into the corresponding amino acids required to build a protein.

Each tRNA molecule has an anticodon region that can base-pair with specific codons (three-nucleotide sequences) on the mRNA. At the other end of the tRNA is the acceptor stem, which contains a binding site for the corresponding amino acid. When an amino acid attaches to the tRNA, it forms an ester bond between the carboxyl group of the amino acid and the 3'-hydroxyl group of the ribose in the tRNA. This aminoacylated tRNA then participates in the translation process, delivering the amino acid to the growing polypeptide chain at the ribosome.

In summary, transfer RNA (tRNA) is a type of RNA molecule that facilitates protein synthesis by transporting and delivering specific amino acids to the ribosome for incorporation into a polypeptide chain, based on the codon-anticodon pairing between tRNAs and messenger RNA (mRNA).

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis in the cell. It carries and transfers specific amino acids to the growing polypeptide chain during translation, the process by which the genetic code in mRNA is translated into a protein sequence.

tRNAs have a characteristic cloverleaf-like secondary structure and a stem-loop tertiary structure, which allows them to bind both to specific amino acids and to complementary codon sequences on the messenger RNA (mRNA) through anticodons. This enables the precise matching of the correct amino acid to its corresponding codon in the mRNA during protein synthesis.

Ser, or serine, is one of the 20 standard amino acids that make up proteins. It is encoded by six different codons (UCU, UCC, UCA, UCG, AGU, and AGC) in the genetic code. The corresponding tRNA molecule that carries serine during protein synthesis is called tRNASer. There are multiple tRNASer isoacceptors, each with a different anticodon sequence but all carrying the same amino acid, serine.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Methionine-tRNA Ligase is an enzyme involved in the process of protein synthesis. Its specific role is to catalyze the attachment of methionine, which is the first amino acid in a newly forming polypeptide chain, to its corresponding transfer RNA (tRNA) molecule. This enzyme binds methionine with a tRNAMet, creating a secure bond that allows for the accurate translation of genetic information from messenger RNA (mRNA) into a protein sequence during translation.

There are two types of Methionine-tRNA Ligases: one for cytoplasmic proteins and another for mitochondrial proteins. These enzymes play crucial roles in initiating protein synthesis within their respective cellular compartments, ensuring proper protein production and maintenance of cellular function.

A codon is a sequence of three adjacent nucleotides in DNA or RNA that specifies the insertion of a particular amino acid during protein synthesis, or signals the beginning or end of translation. In DNA, these triplets are read during transcription to produce a complementary mRNA molecule, which is then translated into a polypeptide chain during translation. There are 64 possible codons in the standard genetic code, with 61 encoding for specific amino acids and three serving as stop codons that signal the termination of protein synthesis.

Transfer RNA (tRNA) that specifically carries the amino acid tyrosine (Tyr) during protein synthesis. In genetic code, Tyr is coded by the codons UAC and UAU. The corresponding anticodon on the tRNA molecule is AUA, which pairs with the mRNA codons to bring tyrosine to the ribosome for incorporation into the growing polypeptide chain.

I'm sorry for any confusion, but "Nucleoside Q" is not a recognized or established term in medical or biological nomenclature. Nucleosides are organic molecules consisting of a pentose sugar (ribose or deoxyribose) linked to a nitrogenous base (adenine, guanine, cytosine, thymine, or uracil). There is no "Q" nucleoside in the standard nomenclature.

If you have any questions about specific nucleosides or related compounds, I'd be happy to try and help clarify those for you!

I believe there may be a slight error in the term you're asking about. "Asp" doesn't specifically relate to RNA (Ribonucleic Acid) or its types. However, I can provide a definition for "Transfer RNA" (tRNA).

Transfer RNA (tRNA) is a type of RNA that plays a crucial role in protein synthesis. It carries and transfers specific amino acids to the growing polypeptide chain during translation, according to the genetic code provided by messenger RNA (mRNA). Each tRNA molecule has an anticodon region which can base-pair with a complementary codon in the mRNA, and a corresponding amino acid attached to its other end. This enables the correct matching of amino acids to form proteins according to the genetic information encoded in mRNA.

Transfer RNA (tRNA) that is specific for the amino acid glutamic acid (Glu or E) is referred to as "tRNA-Glu" or "tRNAGlu." This tRNA carries the amino acid glutamic acid to the ribosome during protein synthesis, where it gets incorporated into a growing polypeptide chain according to the genetic code.

The transfer RNA molecules are small adaptor molecules that facilitate translation of the genetic code present in messenger RNA (mRNA) into the corresponding amino acid sequence of proteins. Each tRNA has an anticodon region, which recognizes and binds to a specific codon on the mRNA through base-pairing interactions. The other end of the tRNA contains a binding site for the corresponding amino acid, ensuring that the correct amino acid is added during protein synthesis.

In summary, "tRNA-Glu" or "tRNAGlu" refers to the specific transfer RNA molecule responsible for transporting and incorporating glutamic acid into proteins during translation.

Pseudouridine is a modified nucleoside that is formed through the enzymatic process of pseudouridylation, where a uracil base in RNA is replaced by a pseudouracil base. Pseudouridine is structurally similar to uridine, but the uracil base is linked to the ribose sugar at carbon-5 rather than carbon-1, which leads to altered chemical and physical properties. This modification can affect RNA structure, stability, and function, and has been implicated in various cellular processes such as translation, splicing, and gene regulation.

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) are a group of enzymes that play a crucial role in protein synthesis. They are responsible for attaching specific amino acids to their corresponding transfer RNAs (tRNAs), creating aminoacyl-tRNA complexes. These complexes are then used in the translation process to construct proteins according to the genetic code.

Each aminoacyl-tRNA synthetase is specific to a particular amino acid, and there are 20 different synthetases in total, one for each of the standard amino acids. The enzymes catalyze the reaction between an amino acid and ATP to form an aminoacyl-AMP intermediate, which then reacts with the appropriate tRNA to create the aminoacyl-tRNA complex. This two-step process ensures the fidelity of the translation process by preventing mismatching of amino acids with their corresponding tRNAs.

Defects in aminoacyl-tRNA synthetases can lead to various genetic disorders and diseases, such as Charcot-Marie-Tooth disease type 2D, distal spinal muscular atrophy, and leukoencephalopathy with brainstem and spinal cord involvement and lactate acidosis (LBSL).

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis, the process by which cells create proteins. In protein synthesis, tRNAs serve as adaptors, translating the genetic code present in messenger RNA (mRNA) into the corresponding amino acids required to build a protein.

tRNAs have a distinct cloverleaf-like secondary structure and a compact L-shaped tertiary structure. Each tRNA molecule contains a specific anticodon triplet nucleotide sequence that can base-pair with a complementary codon in the mRNA during translation. At the other end of the tRNA, there is an amino acid attachment site where the corresponding amino acid is covalently attached through the action of aminoacyl-tRNA synthetase enzymes.

Pro (also known as proline) is a specific amino acid that can be carried by certain tRNAs during protein synthesis. Therefore, in a medical definition context, 'RNA, Transfer, Pro' would refer to the transfer RNA molecule(s) specifically responsible for carrying and delivering proline during protein synthesis. This tRNA is typically denoted as tRNA^Pro^ or tRNA-Pro, with the superscript indicating the specific amino acid it carries.

Transfer RNA (tRNA) that carries the amino acid cysteine (Cys) is a type of adaptor molecule in the process of translation during protein synthesis. The genetic code for cysteine is UGU and UGC, which are the anticodon sequences on specific tRNAs. These tRNA molecules recognize and bind to the corresponding mRNA codons through base-pairing, allowing for the addition of cysteine to the growing polypeptide chain in a ribosome. The tRNA^Cys plays a crucial role in maintaining the fidelity and efficiency of protein synthesis.

A transfer RNA (tRNA) molecule that carries the amino acid leucine is referred to as "tRNA-Leu." This specific tRNA molecule recognizes and binds to a codon (a sequence of three nucleotides in mRNA) during protein synthesis or translation. In this case, tRNA-Leu can recognize and pair with any of the following codons: UUA, UUG, CUU, CUC, CUA, and CUG. Once bound to the mRNA at the ribosome, leucine is added to the growing polypeptide chain through the action of aminoacyl-tRNA synthetase enzymes that catalyze the attachment of specific amino acids to their corresponding tRNAs. This ensures the accurate and efficient production of proteins based on genetic information encoded in mRNA.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Genetic suppression is a concept in genetics that refers to the phenomenon where the expression or function of one gene is reduced or silenced by another gene. This can occur through various mechanisms such as:

* Allelic exclusion: When only one allele (version) of a gene is expressed, while the other is suppressed.
* Epigenetic modifications: Chemical changes to the DNA or histone proteins that package DNA can result in the suppression of gene expression.
* RNA interference: Small RNAs can bind to and degrade specific mRNAs (messenger RNAs), preventing their translation into proteins.
* Transcriptional repression: Proteins called transcription factors can bind to DNA and prevent the recruitment of RNA polymerase, which is necessary for gene transcription.

Genetic suppression plays a crucial role in regulating gene expression and maintaining proper cellular function. It can also contribute to diseases such as cancer when genes that suppress tumor growth are suppressed themselves.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis in the cell. It carries amino acids to the ribosome, where they are joined together in a specific sequence to form a polypeptide chain, which ultimately becomes a protein.

Each tRNA molecule has a unique structure and is responsible for carrying a specific amino acid. The genetic information that specifies which amino acid a particular tRNA carries is encoded in the form of a three-nucleotide sequence called an anticodon, which is located on one end of the tRNA molecule.

Threonine (Thr) is one of the twenty standard amino acids found in proteins. It is encoded by the codons ACU, ACA, ACC, and ACG in the genetic code. Therefore, a tRNA molecule with an anticodon complementary to any of these codons will carry threonine during protein synthesis.

So, to provide a medical definition of 'RNA, Transfer, Thr', it would be: A type of transfer RNA (tRNA) that carries the amino acid threonine (Thr) to the ribosome during protein synthesis and has an anticodon sequence complementary to one or more of the codons ACU, ACA, ACC, or ACG.

Transfer RNA (tRNA) that carries glutamine (Gln) is a type of RNA molecule involved in protein synthesis. Glutamine is one of the twenty standard amino acids used by cells to construct proteins. During protein synthesis, tRNAs serve as adaptors between the mRNA code and the corresponding amino acids. Specifically, the tRNA with the anticodon complementary to the mRNA codon for glutamine (CAA or CAG) binds to glutamine and delivers it to the growing polypeptide chain during translation. This particular tRNA is referred to as 'tRNA Gln' or 'tRNA for Gln'.

Transfer RNA (tRNA) aminoacylation is the process by which an amino acid is chemically linked to a specific tRNA molecule through an ester bond. This reaction is catalyzed by an enzyme called aminoacyl-tRNA synthetase, which plays a crucial role in protein synthesis. Each type of tRNA corresponds to a particular amino acid, and the correct pairing between them ensures that the genetic code carried by messenger RNA (mRNA) is accurately translated into the corresponding amino acid sequence during protein synthesis. This precise matching of tRNAs with their respective amino acids is essential for maintaining the fidelity of the translation process and ultimately, for the proper functioning of proteins in living organisms.

'RNA, Transfer, Ala' refers to a specific type of transfer RNA (tRNA) molecule that is involved in protein synthesis. In molecular biology, the term 'RNA' stands for ribonucleic acid, which is a nucleic acid present in the cells of all living organisms. Transfer RNAs are a type of RNA that help translate genetic information from messenger RNA (mRNA) into proteins during the process of protein synthesis or translation.

'Transfer, Ala' more specifically refers to a transfer RNA molecule that carries the amino acid alanine (Ala) to the ribosome during protein synthesis. Each tRNA has a specific anticodon sequence that can base-pair with a complementary codon sequence in the mRNA, and it also carries a specific amino acid that corresponds to that codon. In this case, the anticodon on the 'Transfer, Ala' tRNA molecule is capable of base-pairing with any one of the three codons (GCU, GCC, GCA, or GCG) that specify alanine in the genetic code.

Therefore, 'RNA, Transfer, Ala' can be defined as a type of transfer RNA molecule that carries and delivers the amino acid alanine to the growing polypeptide chain during protein synthesis.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis in the cell. It carries amino acids to the ribosome, where they are joined together in a specific sequence to form a polypeptide chain, which eventually becomes a protein.

Each tRNA molecule has a unique structure and is responsible for carrying a specific amino acid to the ribosome during protein synthesis. The amino acids are attached to the tRNA at a site called the acceptor stem, which contains a three-base sequence known as the anticodon.

Val (or V) is one of the twenty standard amino acids found in proteins. It stands for Valine, and its codons are GUA, GUC, GUG, and GUU. Therefore, tRNA Val refers to a specific type of transfer RNA molecule that carries valine to the ribosome during protein synthesis.

Isopentenyladenosine (IPA) is a derivative of adenosine, which is a nucleoside consisting of adenine attached to ribose sugar via a β-N9-glycosidic bond. In Isopentenyladenosine, an isopentenyl group (a hydrocarbon chain with five carbon atoms) is added to the N6 position of the adenine base.

Isopentenyladenosine is a key intermediate in the biosynthesis of cytokinins, a class of plant hormones that play crucial roles in cell division and differentiation, shoot initiation, leaf expansion, apical dominance, root growth, and other developmental processes.

It's worth noting that Isopentenyladenosine is not typically used as a medical term or definition but rather in the context of biochemistry and plant physiology.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

The genetic code is the set of rules that dictates how DNA and RNA sequences are translated into proteins. It consists of a 64-unit "alphabet" formed by all possible combinations of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) in DNA or uracil (U) in RNA. These triplets, also known as codons, specify the addition of specific amino acids during protein synthesis or signal the start or stop of translation. This code is universal across all known organisms, with only a few exceptions.

Thiouridine is not a medical term per se, but it is a term used in biochemistry and genetics. Thiouridine is a modified nucleoside that contains a sulfur atom, and it is found in the RNA (ribonucleic acid) of certain organisms, including yeast and mammals.

Thiouridine can be formed through the modification of uridine, one of the four basic building blocks of RNA, by the addition of a sulfur atom from a donor molecule such as cysteine or a derivative thereof. This modification can affect the stability, structure, and function of RNA molecules, including transfer RNAs (tRNAs) and ribosomal RNAs (rRNAs).

In medicine, thiouridine is not used as a therapeutic agent or diagnostic tool, but it may be studied in the context of genetic research or molecular biology.

Bacterial RNA refers to the genetic material present in bacteria that is composed of ribonucleic acid (RNA). Unlike higher organisms, bacteria contain a single circular chromosome made up of DNA, along with smaller circular pieces of DNA called plasmids. These bacterial genetic materials contain the information necessary for the growth and reproduction of the organism.

Bacterial RNA can be divided into three main categories: messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA). mRNA carries genetic information copied from DNA, which is then translated into proteins by the rRNA and tRNA molecules. rRNA is a structural component of the ribosome, where protein synthesis occurs, while tRNA acts as an adapter that brings amino acids to the ribosome during protein synthesis.

Bacterial RNA plays a crucial role in various cellular processes, including gene expression, protein synthesis, and regulation of metabolic pathways. Understanding the structure and function of bacterial RNA is essential for developing new antibiotics and other therapeutic strategies to combat bacterial infections.

Uridine is a nucleoside that consists of a pyrimidine base (uracil) linked to a pentose sugar (ribose). It is a component of RNA, where it pairs with adenine. Uridine can also be found in various foods such as beer, broccoli, yeast, and meat. In the body, uridine can be synthesized from orotate or from the breakdown of RNA. It has several functions, including acting as a building block for RNA, contributing to energy metabolism, and regulating cell growth and differentiation. Uridine is also available as a dietary supplement and has been studied for its potential benefits in various health conditions.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis. It carries amino acids to the ribosome, where they are incorporated into growing polypeptide chains during translation, the process by which the genetic code in mRNA is translated into a protein sequence.

tRNAs have a characteristic cloverleaf-like secondary structure and a stem-loop tertiary structure, which allows them to recognize specific codons on the mRNA through base-pairing between their anticodon loops and the complementary codons. Each tRNA is specific for one amino acid, and there are multiple tRNAs for each amino acid that differ in their anticodon sequences, allowing them to recognize different codons that specify the same amino acid.

"His" refers to the amino acid Histidine, which is encoded by the codons CAU and CAC on mRNA. Therefore, tRNA-His is a type of tRNA molecule that carries the amino acid Histidine to the ribosome during protein synthesis.

Oligoribonucleotides are short, synthetic chains of ribonucleotides, which are the building blocks of RNA (ribonucleic acid). These chains typically contain fewer than 20 ribonucleotide units, and can be composed of all four types of nucleotides found in RNA: adenine (A), uracil (U), guanine (G), and cytosine (C). They are often used in research for various purposes, such as studying RNA function, regulating gene expression, or serving as potential therapeutic agents.

Aminoacylation is a biochemical process in which an amino acid is linked to a transfer RNA (tRNA) molecule through the formation of an ester bond. This reaction is catalyzed by an enzyme called an aminoacyl-tRNA synthetase, which specifically recognizes and activates a particular amino acid and then attaches it to the appropriate tRNA molecule.

The resulting aminoacyl-tRNA complexes are essential for protein synthesis in all living organisms. During translation, the genetic information encoded in messenger RNA (mRNA) is used to direct the sequential addition of amino acids to a growing polypeptide chain. Each aminoacyl-tRNA molecule carries a specific amino acid that corresponds to a particular codon in the mRNA, ensuring that the correct amino acids are added to the protein in the proper order.

Therefore, the process of aminoacylation plays a crucial role in maintaining the fidelity and accuracy of protein synthesis, as well as contributing to the regulation of gene expression and the maintenance of cellular homeostasis.

tRNA (transfer RNA) methyltransferases are a group of enzymes that catalyze the transfer of a methyl group (-CH3) to specific positions on the tRNA molecule. These enzymes play a crucial role in modifying and regulating tRNA function, stability, and interaction with other components of the translation machinery during protein synthesis.

The addition of methyl groups to tRNAs can occur at various sites, including the base moieties of nucleotides within the anticodon loop, the TψC loop, and the variable region. These modifications help maintain the structural integrity of tRNA molecules, enhance their ability to recognize specific codons during translation, and protect them from degradation by cellular nucleases.

tRNA methyltransferases are classified based on the type of methylation they catalyze:

1. N1-methyladenosine (m1A) methyltransferases: These enzymes add a methyl group to the N1 position of adenosine residues in tRNAs. An example is TRMT6/TRMT61A, which methylates adenosines at position 58 in human tRNAs.
2. N3-methylcytosine (m3C) methyltransferases: These enzymes add a methyl group to the N3 position of cytosine residues in tRNAs. An example is Dnmt2, which methylates cytosines at position 38 in various organisms.
3. N7-methylguanosine (m7G) methyltransferases: These enzymes add a methyl group to the N7 position of guanosine residues in tRNAs, primarily at position 46 within the TψC loop. An example is Trm8/Trm82, which catalyzes this modification in yeast and humans.
4. 2'-O-methylated nucleotides (Nm) methyltransferases: These enzymes add a methyl group to the 2'-hydroxyl group of ribose sugars in tRNAs, which can occur at various positions throughout the molecule. An example is FTSJ1, which methylates uridines at position 8 in human tRNAs.
5. Pseudouridine (Ψ) synthases: Although not technically methyltransferases, pseudouridine synthases catalyze the isomerization of uridine to pseudouridine, which can enhance tRNA stability and function. An example is Dyskerin (DKC1), which introduces Ψ at various positions in human tRNAs.

These enzymes play crucial roles in modifying tRNAs, ensuring proper folding, stability, and function during translation. Defects in these enzymes can lead to various diseases, including neurological disorders, cancer, and premature aging.

Ribosomes are complex macromolecular structures composed of ribonucleic acid (RNA) and proteins that play a crucial role in protein synthesis within cells. They serve as the site for translation, where messenger RNA (mRNA) is translated into a specific sequence of amino acids to create a polypeptide chain, which eventually folds into a functional protein.

Ribosomes consist of two subunits: a smaller subunit and a larger subunit. These subunits are composed of ribosomal RNA (rRNA) molecules and proteins. In eukaryotic cells, the smaller subunit is denoted as the 40S subunit, while the larger subunit is referred to as the 60S subunit. In prokaryotic cells, these subunits are named the 30S and 50S subunits, respectively. The ribosome's overall structure resembles a "doughnut" or a "cotton reel," with grooves and binding sites for various factors involved in protein synthesis.

Ribosomes can be found floating freely within the cytoplasm of cells or attached to the endoplasmic reticulum (ER) membrane, forming part of the rough ER. Membrane-bound ribosomes are responsible for synthesizing proteins that will be transported across the ER and ultimately secreted from the cell or inserted into the membrane. In contrast, cytoplasmic ribosomes synthesize proteins destined for use within the cytoplasm or organelles.

In summary, ribosomes are essential components of cells that facilitate protein synthesis by translating mRNA into functional polypeptide chains. They can be found in various cellular locations and exist as either free-floating entities or membrane-bound structures.

Lysine-tRNA ligase is an enzyme involved in the process of protein synthesis, specifically during the step of translation. Its primary function is to catalyze the attachment of the amino acid lysine to its corresponding transfer RNA (tRNA) molecule. This reaction forms a covalent bond between the carboxyl group of the lysine and the 3'-hydroxyl group of the tRNA, creating a charged lysine-tRNA complex.

The resulting complex is then transported to the ribosome, where it participates in the elongation phase of translation. Here, the lysine-tRNA complex binds to the appropriate codon on the mRNA and contributes to the formation of a polypeptide chain. The proper matching of amino acids to their corresponding tRNAs is crucial for maintaining the fidelity of protein synthesis and ensuring that the correct proteins are produced in the cell.

There are two main types of lysine-tRNA ligases: Lys-tRNA^Lys ligase (also known as lysyl-tRNA synthetase) and Lys-tRNA^UUG ligase (also known as bifunctional lysyl-tRNA synthetase). These enzymes differ in their substrate specificity, with the former recognizing tRNA^Lys molecules and the latter recognizing tRNA^UUG molecules. Both enzymes play essential roles in maintaining the accuracy of protein synthesis and ensuring proper cellular function.

Base pairing is a specific type of chemical bonding that occurs between complementary base pairs in the nucleic acid molecules DNA and RNA. In DNA, these bases are adenine (A), thymine (T), guanine (G), and cytosine (C). Adenine always pairs with thymine via two hydrogen bonds, while guanine always pairs with cytosine via three hydrogen bonds. This precise base pairing is crucial for the stability of the double helix structure of DNA and for the accurate replication and transcription of genetic information. In RNA, uracil (U) takes the place of thymine and pairs with adenine.

Protein biosynthesis is the process by which cells generate new proteins. It involves two major steps: transcription and translation. Transcription is the process of creating a complementary RNA copy of a sequence of DNA. This RNA copy, or messenger RNA (mRNA), carries the genetic information to the site of protein synthesis, the ribosome. During translation, the mRNA is read by transfer RNA (tRNA) molecules, which bring specific amino acids to the ribosome based on the sequence of nucleotides in the mRNA. The ribosome then links these amino acids together in the correct order to form a polypeptide chain, which may then fold into a functional protein. Protein biosynthesis is essential for the growth and maintenance of all living organisms.

Ribonucleic acid (RNA) is a type of nucleic acid that plays a crucial role in the process of gene expression. There are several types of RNA molecules, including messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA). These RNA molecules help to transcribe DNA into mRNA, which is then translated into proteins by the ribosomes.

Fungi are a group of eukaryotic organisms that include microorganisms such as yeasts and molds, as well as larger organisms like mushrooms. Like other eukaryotes, fungi contain DNA and RNA as part of their genetic material. The RNA in fungi is similar to the RNA found in other organisms, including humans, and plays a role in gene expression and protein synthesis.

A specific medical definition of "RNA, fungal" does not exist, as RNA is a fundamental component of all living organisms, including fungi. However, RNA can be used as a target for antifungal drugs, as certain enzymes involved in RNA synthesis and processing are unique to fungi and can be inhibited by these drugs. For example, the antifungal drug flucytosine is converted into a toxic metabolite that inhibits fungal RNA and DNA synthesis.

Glycine-tRNA ligase, also known as glycyl-tRNA synthetase, is an enzyme that plays a crucial role in protein synthesis. Its primary function is to catalyze the reaction between the amino acid glycine and its corresponding transfer RNA (tRNA) molecule. This reaction forms a covalent bond between glycine and tRNA, creating a charged tRNA molecule that can then participate in protein synthesis on the ribosome.

The systematic name for this enzyme is "glycyl-tRNA ligase (AMP-forming)" and it belongs to the class II aminoacyl-tRNA synthetases. It requires ATP as a cofactor to activate the glycine molecule before forming the ester bond with tRNA. Defects in this enzyme have been associated with certain neurological disorders, such as Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.

Cytidine is a nucleoside, which consists of the sugar ribose and the nitrogenous base cytosine. It is an important component of RNA (ribonucleic acid), where it pairs with guanosine via hydrogen bonding to form a base pair. Cytidine can also be found in some DNA (deoxyribonucleic acid) sequences, particularly in viral DNA and in mitochondrial DNA.

Cytidine can be phosphorylated to form cytidine monophosphate (CMP), which is a nucleotide that plays a role in various biochemical reactions in the body. CMP can be further phosphorylated to form cytidine diphosphate (CDP) and cytidine triphosphate (CTP), which are involved in the synthesis of lipids, glycogen, and other molecules.

Cytidine is also available as a dietary supplement and has been studied for its potential benefits in treating various health conditions, such as liver disease and cancer. However, more research is needed to confirm these potential benefits and establish safe and effective dosages.

Acylation is a medical and biological term that refers to the process of introducing an acyl group (-CO-) into a molecule. This process can occur naturally or it can be induced through chemical reactions. In the context of medicine and biology, acylation often occurs during post-translational modifications of proteins, where an acyl group is added to specific amino acid residues, altering the protein's function, stability, or localization.

An example of acylation in medicine is the administration of neuraminidase inhibitors, such as oseltamivir (Tamiflu), for the treatment and prevention of influenza. These drugs work by inhibiting the activity of the viral neuraminidase enzyme, which is essential for the release of newly formed virus particles from infected cells. Oseltamivir is administered orally as an ethyl ester prodrug, which is then hydrolyzed in the body to form the active acylated metabolite that inhibits the viral neuraminidase.

In summary, acylation is a vital process in medicine and biology, with implications for drug design, protein function, and post-translational modifications.

Threonine-tRNA ligase is an enzyme that plays a crucial role in protein synthesis, specifically in the attachment of threonine (Thr) to its corresponding transfer RNA (tRNA). This enzyme catalyzes the formation of a ester bond between the carboxyl group of threonine and the 3'-hydroxyl group of the tRNAThr, creating a charged tRNA molecule that can participate in translation at the ribosome. Proper function of threonine-tRNA ligase is essential for maintaining the fidelity and efficiency of protein synthesis, as it ensures that the correct amino acids are incorporated into proteins according to the genetic code.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Ribonucleases (RNases) are a group of enzymes that catalyze the degradation of ribonucleic acid (RNA) molecules by hydrolyzing the phosphodiester bonds. These enzymes play crucial roles in various biological processes, such as RNA processing, turnover, and quality control. They can be classified into several types based on their specificities, mechanisms, and cellular localizations.

Some common classes of ribonucleases include:

1. Endoribonucleases: These enzymes cleave RNA internally, at specific sequences or structural motifs. Examples include RNase A, which targets single-stranded RNA; RNase III, which cuts double-stranded RNA at specific stem-loop structures; and RNase T1, which recognizes and cuts unpaired guanosine residues in RNA molecules.
2. Exoribonucleases: These enzymes remove nucleotides from the ends of RNA molecules. They can be further divided into 5'-3' exoribonucleases, which degrade RNA starting from the 5' end, and 3'-5' exoribonucleases, which start at the 3' end. Examples include Xrn1, a 5'-3' exoribonuclease involved in mRNA decay; and Dis3/RRP6, a 3'-5' exoribonuclease that participates in ribosomal RNA processing and degradation.
3. Specific ribonucleases: These enzymes target specific RNA molecules or regions with high precision. For example, RNase P is responsible for cleaving the 5' leader sequence of precursor tRNAs (pre-tRNAs) during their maturation; and RNase MRP is involved in the processing of ribosomal RNA and mitochondrial RNA molecules.

Dysregulation or mutations in ribonucleases have been implicated in various human diseases, such as neurological disorders, cancer, and viral infections. Therefore, understanding their functions and mechanisms is crucial for developing novel therapeutic strategies.

'Frameshifting, ribosomal' refers to a type of genetic modification that occurs during translation, the process by which messenger RNA (mRNA) is translated into a protein. Specifically, frameshifting is a type of error or programmed change in the reading frame of the mRNA as it is being translated by the ribosome.

In ribosomal frameshifting, the ribosome shifts the reading frame of the mRNA by one or two nucleotides, resulting in an entirely different sequence of amino acids being incorporated into the growing polypeptide chain. This can lead to the production of a truncated or elongated protein, or a completely different protein altogether.

There are two types of ribosomal frameshifting: programmed -1 frameshifting and programmed +1 frameshifting. Programmed -1 frameshifting involves a -1 shift in the reading frame, resulting in the incorporation of a different set of three nucleotides (a codon) into the polypeptide chain. Programmed +1 frameshifting involves a +1 shift in the reading frame, with similar consequences.

Ribosomal frameshifting is a tightly regulated process that plays an important role in gene expression and can have significant consequences for protein function and cellular physiology. It is also implicated in certain genetic diseases and viral infections.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Guanosine is a nucleoside that consists of a guanine base linked to a ribose sugar molecule through a beta-N9-glycosidic bond. It plays a crucial role in various biological processes, such as serving as a building block for DNA and RNA during replication and transcription. Guanosine triphosphate (GTP) and guanosine diphosphate (GDP) are important energy carriers and signaling molecules involved in intracellular regulation. Additionally, guanosine has been studied for its potential role as a neuroprotective agent and possible contribution to cell-to-cell communication.

Ribonuclease T1 is a type of enzyme that belongs to the ribonuclease family. Its primary function is to cleave or cut single-stranded RNA molecules at specific sites, particularly after guanine residues. This enzyme is produced by various organisms, including fungi and humans, and it plays a crucial role in the regulation of RNA metabolism and function.

In particular, Ribonuclease T1 from Aspergillus oryzae is widely used in biochemical and molecular biology research due to its specificity for single-stranded RNA and its ability to cleave RNA molecules into small fragments. This enzyme has been extensively used in techniques such as RNase protection assays, structure probing, and mapping of RNA secondary structures.

Tryptophan-tRNA ligase is an enzyme that plays a crucial role in protein synthesis. Its primary function is to join tryptophan, one of the twenty standard amino acids, to its corresponding transfer RNA (tRNA) molecule. This enzyme catalyzes the formation of a peptide bond between tryptophan and the tRNA during the translation process, where genetic information from messenger RNA (mRNA) is translated into a specific protein sequence. The correct pairing of amino acids with their respective tRNAs is essential for maintaining the fidelity of protein synthesis and ensuring the production of functional proteins.

Glutamate-tRNA ligase is an enzyme involved in the process of protein synthesis, specifically during the charging or aminoacylation of transfer RNA (tRNA). This enzyme is responsible for catalyzing the reaction between glutamic acid (Glu) and its corresponding tRNA molecule (tRNAGlu), forming a covalent bond between them. The resulting product, Glu-tRNAGlu, then participates in the translation of messenger RNA (mRNA) into a specific protein sequence at the ribosome.

The reaction catalyzed by glutamate-tRNA ligase is as follows:

Glutamic acid + ATP + tRNAGlu ↔ Glu-tRNAGlu + AMP + PP~i~ (pyrophosphate)

This enzyme plays a crucial role in maintaining the accuracy and efficiency of protein synthesis, ensuring that the correct amino acids are incorporated into proteins according to the genetic code. Defects or mutations in glutamate-tRNA ligase can lead to various genetic disorders and impairments in cellular function.

Aspartate-tRNA ligase is an enzyme that plays a crucial role in protein synthesis. Its specific function is to join the amino acid aspartic acid to its corresponding transfer RNA (tRNA) molecule, forming an aspartyl-tRNA complex. This complex is essential for the accurate translation of genetic information encoded in messenger RNA (mRNA) into a polypeptide chain during protein synthesis.

The systematic name for this enzyme is L-aspartate:tRNA(Asn) ligase (AMP-forming), which reflects its role in catalyzing the reaction between aspartic acid and tRNA(Asn). The enzyme can also activate aspartic acid by forming an aspartyl-AMP intermediate before transferring the activated aspartate to the appropriate tRNA molecule.

Deficiencies or mutations in aspartate-tRNA ligase can lead to various genetic disorders and impairments in protein synthesis, which may have severe consequences for cellular function and overall health.

A codon is a sequence of three adjacent nucleotides in DNA or RNA that specifies a particular amino acid during the process of protein synthesis, or codes for the termination of translation. In DNA, these triplets are read in a 5' to 3' direction, while in mRNA, they are read in a 5' to 3' direction as well. There are 64 possible codons (4^3) in the genetic code, and 61 of them specify amino acids. The remaining three codons, UAA, UAG, and UGA, are terminator or stop codons that signal the end of protein synthesis.

Terminator codons, also known as nonsense codons, do not code for any amino acids. Instead, they cause the release of the newly synthesized polypeptide chain from the ribosome, which is the complex machinery responsible for translating the genetic code into a protein. This process is called termination or translation termination.

In prokaryotic cells, termination occurs when a release factor recognizes and binds to the stop codon in the A site of the ribosome. This triggers the hydrolysis of the peptidyl-tRNA bond, releasing the completed polypeptide chain from the tRNA and the ribosome. In eukaryotic cells, a similar process occurs, but it involves different release factors and additional steps to ensure accurate termination.

In summary, a codon is a sequence of three adjacent nucleotides in DNA or RNA that specifies an amino acid or signals the end of protein synthesis. Terminator codons are specific codons that do not code for any amino acids and instead signal the end of translation, leading to the release of the newly synthesized polypeptide chain from the ribosome.

Post-transcriptional RNA processing refers to the modifications and regulations that occur on RNA molecules after the transcription of DNA into RNA. This process includes several steps:

1. 5' capping: The addition of a cap structure, usually a methylated guanosine triphosphate (GTP), to the 5' end of the RNA molecule. This helps protect the RNA from degradation and plays a role in its transport, stability, and translation.
2. 3' polyadenylation: The addition of a string of adenosine residues (poly(A) tail) to the 3' end of the RNA molecule. This process is important for mRNA stability, export from the nucleus, and translation initiation.
3. Intron removal and exon ligation: Eukaryotic pre-messenger RNAs (pre-mRNAs) contain intronic sequences that do not code for proteins. These introns are removed by a process called splicing, where the flanking exons are joined together to form a continuous mRNA sequence. Alternative splicing can lead to different mature mRNAs from a single pre-mRNA, increasing transcriptomic and proteomic diversity.
4. RNA editing: Specific nucleotide changes in RNA molecules that alter the coding potential or regulatory functions of RNA. This process is catalyzed by enzymes like ADAR (Adenosine Deaminases Acting on RNA) and APOBEC (Apolipoprotein B mRNA Editing Catalytic Polypeptide-like).
5. Chemical modifications: Various chemical modifications can occur on RNA nucleotides, such as methylation, pseudouridination, and isomerization. These modifications can influence RNA stability, localization, and interaction with proteins or other RNAs.
6. Transport and localization: Mature mRNAs are transported from the nucleus to the cytoplasm for translation. In some cases, specific mRNAs are localized to particular cellular compartments to ensure local protein synthesis.
7. Degradation: RNA molecules have finite lifetimes and undergo degradation by various ribonucleases (RNases). The rate of degradation can be influenced by factors such as RNA structure, modifications, or interactions with proteins.

Base composition in genetics refers to the relative proportion of the four nucleotide bases (adenine, thymine, guanine, and cytosine) in a DNA or RNA molecule. In DNA, adenine pairs with thymine, and guanine pairs with cytosine, so the base composition is often expressed in terms of the ratio of adenine + thymine (A-T) to guanine + cytosine (G-C). This ratio can vary between species and even between different regions of the same genome. The base composition can provide important clues about the function, evolution, and structure of genetic material.

Valine-tRNA Ligase is an enzyme that plays a crucial role in protein synthesis in the body. Its specific function is to catalyze the attachment of the amino acid valine to its corresponding transfer RNA (tRNA) molecule during translation, the process by which genetic information encoded in messenger RNA (mRNA) is used to synthesize proteins.

The reaction catalyzed by Valine-tRNA Ligase involves the activation of valine through the formation of an adenylate intermediate with ATP, followed by the transfer of valine to the appropriate tRNA molecule. This enzyme is essential for maintaining the fidelity and efficiency of protein synthesis, as it ensures that the correct amino acid is incorporated into the growing polypeptide chain during translation.

Valine-tRNA Ligase is a member of the class II aminoacyl-tRNA synthetases and contains several functional domains, including an anticodon-binding domain that recognizes and binds to specific tRNA molecules, and a catalytic domain that carries out the reaction with valine. Mutations in the gene encoding Valine-tRNA Ligase have been associated with various genetic disorders, highlighting its importance in maintaining normal cellular function.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Tyrosine-tRNA ligase is an enzyme that plays a crucial role in protein synthesis, specifically in the process of translating the genetic code from messenger RNA (mRNA) into proteins. More formally known as tyrosyl-tRNA synthetase, this enzyme is responsible for charging tRNA molecules with their specific amino acids. In this case, it catalyzes the attachment of the amino acid tyrosine to its corresponding transfer RNA (tRNA) molecule. This enzymatic reaction involves the activation of tyrosine with ATP to form an aminoacyl-AMP intermediate, followed by the transfer of the tyrosyl group from the intermediate to the 3' end of its appropriate tRNA. The resulting tyrosine-tRNA complex is then used in the translation process to incorporate tyrosine into the growing polypeptide chain during protein synthesis.

Transfer RNA (tRNA) that carries asparagine (Asn) is a type of RNA molecule that plays a crucial role in protein synthesis. Specifically, tRNAs are responsible for delivering the appropriate amino acids to the ribosome during translation, the process by which genetic information encoded in messenger RNA (mRNA) is translated into proteins.

In the case of tRNA-Asn, this RNA molecule carries the amino acid asparagine, which is one of the 20 standard amino acids used to build proteins. The tRNA-Asn molecule recognizes a specific codon (a sequence of three nucleotides) in the mRNA that corresponds to asparagine, and then brings the appropriate amino acid to the ribosome to be incorporated into the growing polypeptide chain.

The correct pairing of tRNAs with their corresponding codons is facilitated by anticodon loops present on the tRNA molecules, which contain complementary sequences to the codons in the mRNA. In the case of tRNA-Asn, the anticodon loop contains the sequence UGU, which is complementary to the asparagine codons AAU and AAC in the mRNA.

Overall, tRNAs like tRNA-Asn are essential for the accurate and efficient synthesis of proteins in all living organisms.

Arginine-tRNA ligase is an enzyme that plays a crucial role in protein synthesis. Its primary function is to join arginine, an essential amino acid, to its corresponding transfer RNA (tRNA) molecule. This enzyme catalyzes the formation of a peptide bond between the arginine and the tRNA during translation, the process by which genetic information encoded in messenger RNA (mRNA) is converted into a protein sequence.

The reaction catalyzed by arginine-tRNA ligase involves two main steps:

1. Activation of arginine: The enzyme binds to and activates an arginine molecule by attaching adenosine triphosphate (ATP) to it, forming an arginine-AMP intermediate.
2. Transfer of arginine to tRNA: The activated arginine is then transferred from the arginine-AMP complex onto the appropriate tRNA molecule, releasing AMP and forming an ester bond between the carboxyl group of arginine and the 3'-hydroxyl group of the ribose moiety in the tRNA.

The resulting arginine-tRNA complex is now ready to participate in protein synthesis, where it will contribute to the formation of a polypeptide chain under the direction of mRNA. The enzyme's role in ensuring accurate amino acid attachment to their corresponding tRNAs is essential for maintaining proper protein folding and function.

There are two main types of arginine-tRNA ligases, based on their structure and mechanism:

1. Class I arginine-tRNA ligase (also known as ArgRS): This enzyme contains an alpha/beta Rossmann-fold domain that binds ATP and a catalytic domain with a characteristic HIGH motif. It follows the standard two-step reaction mechanism for class I aminoacyl-tRNA synthetases.
2. Class II arginine-tRNA ligase (also known as ArgQ): This enzyme has an alpha/beta/alpha sandwich fold and a distinct catalytic mechanism compared to Class I enzymes. It follows the three-step reaction mechanism for class II aminoacyl-tRNA synthetases, which includes an intermediate step of adenylate formation before transferring arginine to tRNA.

Both types of arginine-tRNA ligases are found in various organisms, including bacteria and eukaryotes. In humans, the Class I enzyme is encoded by the RARS gene, while the Class II enzyme is encoded by the QARS gene. Dysfunction or mutations in these genes can lead to neurological disorders and other health issues due to impaired protein synthesis and folding.

Phenylalanine-tRNA ligase, also known as Phe-tRNA synthetase, is an enzyme that plays a crucial role in protein synthesis. Its primary function is to catalyze the attachment of the amino acid phenylalanine to its corresponding transfer RNA (tRNA) molecule. This reaction forms a phenylalanine-tRNA complex, which is then used in the translation process to create proteins according to the genetic code. The systematic name for this enzyme is phenylalanyl-tRNA synthetase (EC 6.1.1.20). Any defects or mutations in the Phe-tRNA ligase can lead to various medical conditions, including neurological disorders and impaired growth.

Serine-tRNA ligase is an enzyme that plays a crucial role in protein synthesis, specifically in the attachment of the amino acid serine to its corresponding transfer RNA (tRNA) molecule. This enzyme catalyzes the formation of a ester bond between the carboxyl group of L-serine and the 3'-hydroxyl group of the tRNASerine, creating a charged tRNASerine molecule that can participate in protein synthesis on the ribosome.

The systematic name for this enzyme is L-serine:tRNA(Ser) ligase (AMP-forming), and it belongs to the family of ligases, specifically the transfer RNA ligases, which form aminoacyl-tRNA and related compounds. This enzyme is essential for maintaining the accuracy and fidelity of protein synthesis, as it ensures that the correct amino acid is attached to its corresponding tRNA molecule before being translated into a polypeptide chain on the ribosome.

Isoleucine-tRNA ligase is an enzyme involved in the process of protein synthesis in cells. Its specific role is to catalyze the attachment of the amino acid isoleucine to its corresponding transfer RNA (tRNA) molecule, which then participates in the translation of genetic information from messenger RNA (mRNA) into a polypeptide chain during protein synthesis. This enzyme helps ensure that the correct amino acids are incorporated into proteins according to the genetic code.

... in which the ribosomal P-site tRNA anticodon re-pairs from XXY to XXX and the A-site anticodon re-pairs from YYH to YYY ... In this model, the motif structure is explained by the fact that the first and second positions of the anticodons must be able ... This difference does not significantly disfavor anticodon binding because the third nucleotide in a codon, known as the wobble ... Crick FH (August 1966). "Codon-anticodon pairing: the wobble hypothesis". Journal of Molecular Biology. 19 (2): 548-555. doi: ...
Crick FH (August 1966). "Codon--anticodon pairing: the wobble hypothesis" (PDF). Journal of Molecular Biology. 19 (2): 548-55. ...
... if one amino acid is coded for by multiple anticodons and those anticodons differ in either the second or third position (first ... anticodon position is necessary for small conformational adjustments that affect the overall pairing geometry of anticodons of ... He postulated that the 5' base on the anticodon, which binds to the 3' base on the mRNA, was not as spatially confined as the ... When reading 5' to 3' the first nucleotide in the anticodon (which is on the tRNA and pairs with the last nucleotide of the ...
... and anticodon-arms. These interactions within tRNA orient the anticodon stem perpendicularly to the amino-acid stem, leading to ... Incorrect codon-anticodon pairs will present distorted helical geometry, which will prevent the A-minor interaction from ... An interesting example of A-minor is its role in anticodon recognition. The ribosome must discriminate between correct and ... Yoshizawa S, Fourmy D, Puglisi JD (September 1999). "Recognition of the codon-anticodon helix by ribosomal RNA". Science. 285 ( ...
Recognition of stop codons in bacteria have been associated with the so-called 'tripeptide anticodon', a highly conserved amino ... Ito, Koichi; Uno, Makiko; Nakamura, Yoshikazu (1999). "A tripeptide 'anticodon' deciphers stop codons in messenger RNA". Nature ... it was shown that the tripeptide anticodon hypothesis is an oversimplification. Stop codons were historically given many ...
Anticodon modifications are important for proper decoding of mRNA. Since the genetic code is degenerate, anticodon ... For example, in eukaryotes an adenosine at position 34 of the anticodon can be converted to inosine. Inosine is a modification ... Another commonly modified base in tRNA is the position adjacent to the anticodon. Position 37 is often hypermodified with bulky ... Modifications in tRNA play crucial roles in maintaining translation efficiency through supporting structure, anticodon-codon ...
In bacteria, the hyper-modified nucleobase queuine takes up the first anticodon position, or its wobble position in the tRNA of ... Universal presence of nucleoside O in the first position of the anticodons of these transfer ribonucleic acid". Biochemistry. ... Harada, Fumio; Nishimura, Susumu (January 1972). "Possible anticodon sequences of tRNAHis, tRNAAsn, and tRNAAsp from ... Queuine is involved in the anticodon sequence of certain tRNA. ... While preQ1 was first discovered as an anticodon sequence of ...
Wrede P, Rich A (November 1979). "Stability of the unique anticodon loop conformation of E.coli tRNAfMet". Nucleic Acids ...
Cochella, L. (2005-05-20). "An Active Role for tRNA in Decoding Beyond Codon:Anticodon Pairing". Science. 308 (5725): 1178-1180 ...
As a graduate student in Paul Doty's lab, Uhlenbeck showed that the anticodon of tRNA was accessible to hybridization to ... Uhlenbeck, Olke C.; Baller, Julie; Doty, Paul (1970). "Complementary Oligonucleotide Binding to the Anticodon Loop of fMet- ...
This region interacts with the wobble base in the anticodon of tRNA. This leads to misreading of mRNA, so incorrect amino acids ...
In eukaryotic organisms, it is found only in position 37, 3'-adjacent to the anticodon, of phenylalanine tRNA. Wybutosine ... Stuart, JW; Koshlap, KM; Guenther, R; Agris, PF (2003). "Naturally-occurring modification restricts the anticodon domain ... as well as generating an anticodon loop for decoding. The wybutosine modification of tRNAPhe is found to be conserved in ... which help to restrict the flexibility of the anticodon. It has been found that when tRNAPhe lacks wybutosine, increased ...
... phosphate The enzyme acetylates the wobble base C34 of the CAU anticodon of elongation-specific tRNAMet. Ikeuchi Y, Kitahara K ... "RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon". The EMBO Journal. 28 (9): 1362-73. doi: ... Suzuki T (August 2008). "The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon". ...
The initiation of mRNA translation involves the placement of the start codon in the P-site through the codon-anticodon base ... IF3 checks P-site codon-anticodon pairing and rejects incorrect initiation complexes. The orderly mechanism of initiation ... A major function of IF3 is inspecting codon-anticodon pairing at the P-site during start codon selection. It accelerates the ... matching with the tRNA anti-codon. IF2 regulates start codon selection accuracy and inhibits elongator tRNAs' binding by ...
Erives A (August 2011). "A model of proto-anti-codon RNA enzymes requiring L-amino acid homochirality". Journal of Molecular ...
Thus, a curious aspect of this model is that the (anti-) codon table is determined in evolutionary history prior to the origin ... Erives A (2011). "A Model of Proto-Anti-Codon RNA Enzymes Requiring L-Amino Acid Homochirality". Journal of Molecular Evolution ... Using insights gleaned from archaeal genomes, Erives elaborated and described a stereochemical model of "proto-anti-codon RNAs ... The pacRNA model explicitly lists possible interactions between various anti-codon di-nucleotide and tri-nucleotide sequences ...
1993). "Structural arrangement of the codon-anticodon interaction area in human placenta ribosomes. Affinity labelling of the ...
1993). "Structural arrangement of the codon-anticodon interaction area in human placenta ribosomes. Affinity labelling of the ...
At the AUG codon a Methionine tRNA anticodon is recognized by mRNA codon. Upon base pairing to the start codon the eIF5 in the ... This stalling allows the start codon and the corresponding anticodon time to form the correct hydrogen bonding. The Kozak ...
1993). "Structural arrangement of the codon-anticodon interaction area in human placenta ribosomes. Affinity labelling of the ...
Erives A (August 2011). "A model of proto-anti-codon RNA enzymes requiring L-amino acid homochirality". Journal of Molecular ... They signal release of the nascent polypeptide from the ribosome because no cognate tRNA has anticodons complementary to these ... the genetic code is a result of a high affinity between each amino acid and its codon or anti-codon; the latter option implies ...
Erives A (August 2011). "A model of proto-anti-codon RNA enzymes requiring L-amino acid homochirality". Journal of Molecular ...
1993). "Structural arrangement of the codon-anticodon interaction area in human placenta ribosomes. Affinity labelling of the ...
Dalgarno L, Shine J (1973). "Conserved terminal sequence in 18S rRNA may represent terminator anticodons". Nature. 245 (148): ...
Dalgarno, L.; Shine, J. (31 October 1973). "Conserved Terminal Sequence in 18S rRNA May Represent Terminator Anticodons". ...
tRNAs have a site for amino acid attachment, and a site called an anticodon. The anticodon is an RNA triplet complementary to ... The ribosome facilitates decoding by inducing the binding of complementary tRNA anticodon sequences to mRNA codons. The tRNAs ... Aminoacyl tRNA synthetases (enzymes) catalyze the bonding between specific tRNAs and the amino acids that their anticodon ... where mRNA codons are matched through complementary base pairing to specific tRNA anticodons. Aminoacyl-tRNA synthetases that ...
In the anticodon stem-loop (ASL) Ψ seems critical for proper binding of tRNAs to the ribosome. Ψ stabilizes the dynamic ... Ψ is commonly found in the D stem and anticodon stem and loop of tRNAs from each domain. In each structural motif the unique ... The stabilized conformation of the ASL helps maintain correct anticodon-codon pairings during translation. This stability may ... accuracy by decreasing the rate of peptide bond formation and allowing for more time for incorrect codon-anticodon pairs to be ...
The anticodon loop is a 5-bp stem whose loop contains the anticodon. The tRNA 5′-to-3′ primary structure contains the anticodon ... Some anticodons pair with more than one codon due to wobble base pairing. Frequently, the first nucleotide of the anticodon is ... One end of the tRNA matches the genetic code in a three-nucleotide sequence called the anticodon. The anticodon forms three ... An anticodon is a unit of three nucleotides corresponding to the three bases of an mRNA codon. Each tRNA has a distinct ...
In tRNAs, this modification stabilizes the secondary structure and influences anticodon stem-loop conformation. In rRNAs, m5C ...
"Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea". Nature Chemical Biology. 6 (4): 277 ...
The meaning of ANTICODON is a triplet of nucleotide bases in transfer RNA that identifies the amino acid carried and binds to a ... The first known use of anticodon was in 1965 See more words from the same year ... "Anticodon." Merriam-Webster.com Dictionary, Merriam-Webster, https://www.merriam-webster.com/dictionary/anticodon. Accessed 30 ...
Joji (George Miller) once known for his controversial videos on his YouTube channel Filthy Frank has finally decided to leave his career in comedy
Anticodon. This slot contains a string as a single value, which lists the three letters that make up the anticodon bases on the ... which list the three letters that make up the base triplets recognized by the anticodon on the tRNA. The direction in which the ...
... the data suggest that the anticodon of tRNA(Lys) harbours anticodon nuclease identity elements and implicates a conserved ... the data suggest that the anticodon of tRNA(Lys) harbours anticodon nuclease identity elements and implicates a conserved ... the data suggest that the anticodon of tRNA(Lys) harbours anticodon nuclease identity elements and implicates a conserved ... the data suggest that the anticodon of tRNA(Lys) harbours anticodon nuclease identity elements and implicates a conserved ...
Homo sapiens (human) tRNA-Val (anticodon AAC) 1-1 (TRV-AAC1 1 to 5) sequence is a product of tRNA-Val-AAC-1-1, tRNA-Val-AAC-1-2 ... Homo sapiens (human) tRNA-Val (anticodon AAC) 1-1 (TRV-AAC1 1 to 5) URS000061D582_9606 *73 nucleotides ...
Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches.. Publication Type:. ... We find that when the mismatch occurs in the second position of the P-site codon-anticodon interaction, the first nucleotide of ... The mRNA codon and the tRNA anticodon interaction is extensively monitored by the ribosome to ensure accuracy in tRNA selection ... Home » Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches. ...
tRNA contains ribonucleotides triplet called anticodon. 7.3. Anti codon base pair with codon. 7.4. An amino acid will be added ...
... in which the ribosomal P-site tRNA anticodon re-pairs from XXY to XXX and the A-site anticodon re-pairs from YYH to YYY ... In this model, the motif structure is explained by the fact that the first and second positions of the anticodons must be able ... This difference does not significantly disfavor anticodon binding because the third nucleotide in a codon, known as the wobble ... Crick FH (August 1966). "Codon-anticodon pairing: the wobble hypothesis". Journal of Molecular Biology. 19 (2): 548-555. doi: ...
Anticodon. A codon is a DNA or RNA sequence of three nucleotides (a trinucleotide) that forms a unit of genetic information ... An anticodon is a trinucleotide sequence located at one end of a transfer RNA (tRNA) molecule, which is complementary to a ... Each time an amino acid is added to a growing polypeptide during protein synthesis, a tRNA anticodon pairs with its ...
IPR036621 Anticodon-binding domain superfamily. IPR045864 Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and ...
What does the anticodon match up to when it joins the chain? ...
Sex-linked inheritance refers to the pattern of inheritance in which a gene for a trait is located on the X-chromosome. This means that the trait is more commonly seen in males, as they only have one X-chromosome, while females have two. If a male inherits a recessive allele for a sex-linked disorder, he will express the disorder because there is no second X-chromosome to mask the effects. Females, on the other hand, need to inherit two recessive alleles to express the disorder. This pattern of inheritance accounts for the higher prevalence of certain disorders in males ...
tRNAsynth_1a_anticodon-bd. UniProtKB/TrEMBL. Val/Leu/Ile-tRNA-synth_edit. UniProtKB/TrEMBL. ...
The Biology of Anticodon Stem-Loop Modifications of Yeast tRNAs. Advisor: Eric Phizicky, Ph.D. ...
Timeline for Protein Lysyl-tRNA synthetase (LysRS) from b.40.4.1: Anticodon-binding domain: *Protein Lysyl-tRNA synthetase ( ... Family b.40.4.1: Anticodon-binding domain [50250] (2 proteins). barrel, closed; n=5, S=10. ... Protein Lysyl-tRNA synthetase (LysRS) from b.40.4.1: Anticodon-binding domain appears in the current release, SCOPe 2.08. ... Protein Lysyl-tRNA synthetase (LysRS) from b.40.4.1: Anticodon-binding domain appears in SCOPe 2.02. *Protein Lysyl-tRNA ...
tRNA-Thr (anticodon TGT) 3-1. Gene Type: tRNA Organism: Homo sapiens Chromosome: 14 NCBI GeneID: 7237 Location: 14q11.2 Also ...
ferredoxin-fold anticodon binding domain containing 1. protein-coding. FANCD2OS. FANCD2 opposite strand. protein-coding. ...
Anticodons air with codons to bring the specific amino acid to the correct place. A second tRNA repeats this process and the ... A tRNA molecule has two ends: one that has a specific binding site for a particular sequence of nucleotides, an anticodon that ...
Fold c.51: Anticodon-binding domain-like [52953] (6 superfamilies). 3 layers: a/b/a; mixed beta-sheet of five strands, order ...
An amino acyl-tRNA (anti-codon = UAC) with an attached methionine comes into the P-site of the ribosome. ... An amino acyl-tRNA (anti-codon = AAA) with an attached phenylalanine comes into the A-site of the ribosome. ... An amino acyl-tRNA (anti-codon) with an attached threonine comes into the A-site of the ribosome. ...
Rould, M.A., Perona, J.J., Steitz, T.A. (1991) Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. ...
Any idea how T-RNAs can find their anti-codon so fast in-vivo? What are the thermodynamics behind this feat? What are the ...
transfer RNA methionine 16 (anticodon CAU). *transfer RNA-Met (CAT) 5-1 ...
Journal Article] Biogenesis and growth phase-dependent alteration of 5-methoxycarbonylmethoxyuridine in tRNA anticodons2016. * ...
  • The mRNA codon and the tRNA anticodon interaction is extensively monitored by the ribosome to ensure accuracy in tRNA selection. (anl.gov)
  • This difference does not significantly disfavor anticodon binding because the third nucleotide in a codon, known as the wobble position, has weaker tRNA anticodon binding specificity than the first and second nucleotides. (wikipedia.org)
  • Each time an amino acid is added to a growing polypeptide during protein synthesis, a tRNA anticodon pairs with its complementary codon on the mRNA molecule, ensuring that the appropriate amino acid is inserted into the polypeptide. (genome.gov)
  • Powered by ATP hydrolysis, the complex then moves from 5ʹ to 3ʹ direction, with the tRNA anticodon searching for the first AUG sequence on the mRNA. (jove.com)
  • We find that when the mismatch occurs in the second position of the P-site codon-anticodon interaction, the first nucleotide of the A-site codon flips from the mRNA path to engage highly conserved 16S rRNA nucleotide A1493 in the decoding center. (anl.gov)
  • A 4-thio-rU modified RNA pentamer was used to study the effect of this modification on codon-anticodon interaction when it is in the wobble position of tRNA. (fishersci.com)
  • Transcribe the following DNA strand into mRNA and translate that strand into a polypeptide chain, identifying the codons, anticodons, and amino acid sequence. (qualitypaperhelp.com)
  • Aminoacyl tRNA synthetase (AATS), the enzyme that chemically binds a tRNA to an amino acid via a high-energy bond, recognises the anticodon loop. (edu.vn)
  • The pairing of a tRNA with its cognate amino acid is crucial, as it ensures that only the particular amino acid matching the anticodon of the tRNA, and in turn matching the codon of the mRNA, is used during protein synthesis. (edu.vn)
  • Due to the degeneracy of the genetic code, multiple tRNAs will have the same amino acid but different anticodons. (edu.vn)
  • An anticodon is a trinucleotide sequence located at one end of a transfer RNA (tRNA) molecule, which is complementary to a corresponding codon in a messenger RNA (mRNA) sequence. (genome.gov)
  • Complementation of a 3-nucleotide codon in a messenger RNA (mRNA) by a 3-nucleotide anticodon of the tRNA results in protein synthesis based on the mRNA code. (edu.vn)
  • We have recently reported that point mutations in the tRNA(Leu) (UUR) and tRNA(Lys) genes cause a defect in the normal modification at the first nucleotide of the anticodon. (elsevierpure.com)
  • Together with recent crystal structures of ASL (Val3) UAC-cmo (5)U 34;m (6)A 37 bound to all four of the valine codons in the A-site of the ribosome's 30S subunit, these results clearly demonstrate that the xo (5)U 34-type modifications order the anticodon loop prior to A-site codon binding for an expanded codon reading, possibly reducing an entropic energy barrier to codon binding. (ncsu.edu)
  • The modification contributes to the tRNA's anticodon domain structure, thermodynamic properties and its ability to bind codons AUA and AUG in translational initiation and elongation. (ncsu.edu)
  • Correct codon-anticodon pairing promotes translational fidelity, with these interactions greatly facilitated by modified nucleosides found in tRNA. (nih.gov)
  • Especially, those occurring within the anticodon often modulate translational efficiency. (bvsalud.org)
  • Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches. (anl.gov)
  • How Mutations in tRNA Distant from the Anticodon Affect the Fidelity of Decoding. (expasy.org)
  • The latency is a result of a masking interaction between the anticodon nuclease core-polypeptide PrrC and the Type IC DNA restriction-modification enzyme EcoprrI. (tau.ac.il)
  • Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding. (ncsu.edu)
  • Upon codon-anticodon recognition, GTP is hydrolyzed and the initiation factors dissociate, allowing the large ribosomal subunit to join the complex and form an intact ribosome. (jove.com)
  • Functional recognition of the modified human tRNA(UUU)(Lys3) anticodon domain by HIV's nucleocapsid protein and a peptide mimic. (ncsu.edu)
  • Random mutagenesis of the low-G + C portion encoding PrrC residues 200-313 was performed, followed by selection for loss of anticodon nuclease-dependent lethality and production of full-sized PrrC-like protein. (tau.ac.il)
  • The contributions of this important modification to the structures and codon binding affinities of the unmodified and fully modified anticodon stem and loop domains of tRNA (Val3) UAC (ASL (Val3) UAC) were elucidated. (ncsu.edu)
  • We report the first synthesis and analyses of the tRNA's anticodon stem and loop domain containing the 5-formylcytidine modification. (ncsu.edu)
  • Because a major determinant in the recognition of tRNAMet by the MetRS is thought to lie in the anticodon sequence that is unchanged (36Schulman L.H. Pelka H. Science. (ncsu.edu)
  • Taken together, the data suggest that the anticodon of tRNA(Lys) harbours anticodon nuclease identity elements and implicates a conserved region in PrrC in their recognition. (tau.ac.il)
  • James PA, Cader MZ, Muntoni F, Childs AM, Crow YJ, Talbot K. Severe childhood SMA and axonal CMT due to anticodon binding domain mutations in the GARS gene. (medlineplus.gov)
  • The accuracy and efficiency with which tRNA decodes genomic information into proteins require posttranscriptional modifications in or adjacent to the anticodon. (ncsu.edu)
  • However, the UV hyperchromicity, circular dichroism ellipticity, and structural analyses indicated that the anticodon modifications enhanced order in the loop. (ncsu.edu)
  • Moreover, the structure illustrates that the enzyme senses exclusively the anticodon arm region of the substrate tRNA and examines the presence of key determinants, 5-carboxymethoxyuridine at position 34 and guanosine at position 35, offering molecular basis for the discriminatory mechanism against non-cognate tRNAs. (bvsalud.org)
  • The first position of the anticodon contains the rare modified base 5-formylcytidine. (ncsu.edu)
  • In this report, we present the X-ray crystal structure of Escherichia coli CmoM complexed with tRNASer1, which contains 5-carboxymethoxyuridine at the 5'-end of anticodon (the 34th position of tRNA). (bvsalud.org)
  • The A4435G mutation leads to the change of A37 to G37 in the anticodon loop of the tRNA (21Qu J. Li R. Zhou X. Tong Y. Lu F. Qian Y. Hu Y. Mo J.Q. West C.E. Guan M.X. Investig. (ncsu.edu)
  • Anticodon loop b. (edu.vn)
  • In this model, the motif structure is explained by the fact that the first and second positions of the anticodons must be able to pair perfectly in both the 0 and −1 frames. (wikipedia.org)
  • The tRNA(Lys)-specific anticodon nuclease exists in latent form in Escheri chia coli strains containing the optional prr locus. (tau.ac.il)
  • Contrary to proposed distal contacts to the tRNA elbow region, stem II locally reinforces the codon-anticodon interactions between stem I and tRNA, achieving low-nanomolar affinity. (nih.gov)
  • Yeast tRNAAsp: codon and wobble codon-anticodon interactions. (nih.gov)
  • Unexpectedly, the Stem II domain acts to locally reinforce the codon-anticodon interactions between Stem I and tRNA. (nih.gov)
  • covelantely attach the proper amino acid to a specific tRNA molecule by recognizing specific bases in the acceptor stem, anticodon stem, or anticodon of tRNAs. (flashcardmachine.com)
  • the anticodon stem and acceptor stem appear to contain no essential elements. (caltech.edu)
  • Between the 5' anticodon-binding stem I domain and the 3' amino acid sensing domains of most T-boxes lies the stem II domain of unknown structure and function. (nih.gov)
  • The type of oxidation product formed in the anticodon stem-loop region varied with the modification type, status, and whether the tRNA was inside or outside the cell during exposure. (nih.gov)
  • The structure also illustrates why tRNA recognition by PylRS is anticodon independent: the anticodon does not contact the enzyme. (broadinstitute.org)
  • The enzyme induces a large deformation of the anticodon loop, resulting in an interaction between two adjacent anticodon bases, which accounts for their prominent role in tRNA identity and translational regulation. (proteopedia.org)
  • James PA, Cader MZ, Muntoni F, Childs AM, Crow YJ, Talbot K. Severe childhood SMA and axonal CMT due to anticodon binding domain mutations in the GARS gene. (medlineplus.gov)
  • Both stems rest against a compact pseudoknot, dock via an extended ribose zipper and jointly create a binding groove specific to the anticodon of its cognate tRNA. (nih.gov)
  • Each codon has a complementary codon called an anticodon on a tRNA molecule. (cliffsnotes.com)
  • prime However, due to the fact this is the complementary to the codon and the simplicity site, the only nucleic acid that are aware that they are actually refer to when we read it at 3' prime to 5' prime, is the anticodon. (ostatic.com)
  • The research group led by Assistant Professor Asuteka Nagao and Professor Tsutomu Suzuki of the Department of Chemistry and Biotechnology at the University of Tokyo's Graduate School of Engineering analyzed mitochondrial tRNA Lys isolated from the Mesocentrotus nudus sea urchin, and discovered a novel modified base, hydroxyl- N 6 -threonylcarbamoyladenosine (ht 6 A), in a part adjacent to the anticodon. (u-tokyo.ac.jp)
  • Vervolgens zal het anti-codon van het methionine tRNA koppelen met het AUG-codon en de grote ribosomale subunit rekruteren. (jove.com)
  • Here, we report a patient with a missense variant of unknown significance predicted to modify residue 308 in the anticodon binding domain of YARS1 (p.Asp308Tyr). (nih.gov)
  • It has been shown that EF-G/EF-2_IV domain mimics the shape of anticodon arm of the tRNA in the structurally homologous ternary complex of Petra, EF-Tu (another transcriptional elongation factor) and GTP analog. (nih.gov)
  • The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, implying that EF-G/EF-2 displaces the A-site tRNA to the P-site by physical interaction with the anticodon arm. (nih.gov)
  • Ribosomen, transfer-RNA (tRNA) en andere eiwitten zijn betrokken bij de productie van de keten van aminozuren - de polypeptide. (jove.com)
  • Agency go super funk with their classic-track-inspired new release, "Super VGA" on Anticodon, one of the coolest labels in 2020, across two mixes, the Original and the Radio Edit. (kingsofspins.com)
  • For your convenience, there is a search service on the main page of the site that would help you find images similar to anticodon clipart with nescessary type and size. (clipground.com)