Aminoacylation
Amino Acyl-tRNA Synthetases
Anticodon
RNA, Transfer, Cys
RNA, Transfer, Amino Acyl
RNA, Transfer
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.
Phenylalanine-tRNA Ligase
Isoleucine-tRNA Ligase
RNA, Transfer, Ala
RNA, Transfer, Leu
Methionine-tRNA Ligase
RNA, Transfer, Asp
RNA, Transfer, Val
Aspartate-tRNA Ligase
RNA, Transfer, Ile
Glutamate-tRNA Ligase
Nucleic Acid Conformation
RNA, Transfer, Pro
RNA, Transfer, Amino Acid-Specific
Tryptophan-tRNA Ligase
RNA, Transfer, Ser
RNA, Transfer, Trp
Escherichia coli
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.
RNA, Transfer, Thr
RNA, Transfer, Met
RNA, Transfer, Glu
RNA, Transfer, Asn
RNA, Transfer, Gln
RNA, Transfer, Arg
RNA, Transfer, His
RNA, Transfer, Tyr
RNA, Transfer, Phe
RNA Editing
A process that changes the nucleotide sequence of mRNA from that of the DNA template encoding it. Some major classes of RNA editing are as follows: 1, the conversion of cytosine to uracil in mRNA; 2, the addition of variable number of guanines at pre-determined sites; and 3, the addition and deletion of uracils, templated by guide-RNAs (RNA, GUIDE).
RNA, Transfer, Gly
Histidine-tRNA Ligase
Base Sequence
RNA, Bacterial
Molecular Sequence Data
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.
RNA, Transfer, Lys
Genetic Code
Phenylalanine
Substrate Specificity
Saccharomyces cerevisiae
Valine
Isoleucine
Amino Acids
Protein Biosynthesis
Tymovirus
Amination
Thermus thermophilus
Methanobacteriaceae
MELAS Syndrome
A mitochondrial disorder characterized by focal or generalized seizures, episodes of transient or persistent neurologic dysfunction resembling strokes, and ragged-red fibers on muscle biopsy. Affected individuals tend to be normal at birth through early childhood, then experience growth failure, episodic vomiting, and recurrent cerebral insults resulting in visual loss and hemiparesis. The cortical lesions tend to occur in the parietal and occipital lobes and are not associated with vascular occlusion. VASCULAR HEADACHE is frequently associated and the disorder tends to be familial. (From Joynt, Clinical Neurology, 1992, Ch56, p117)
Mutation
MERRF Syndrome
A mitochondrial encephalomyopathy characterized clinically by a mixed seizure disorder, myoclonus, progressive ataxia, spasticity, and a mild myopathy. Dysarthria, optic atrophy, growth retardation, deafness, and dementia may also occur. This condition tends to present in childhood and to be transmitted via maternal lineage. Muscle biopsies reveal ragged-red fibers and respiratory chain enzymatic defects. (From Adams et al., Principles of Neurology, 6th ed, p986)
Models, Molecular
Adenosine Monophosphate
Binding Sites
Oligoribonucleotides
N-Formylmethionine
Amino Acid Sequence
RNA Ligase (ATP)
Adenosine Triphosphate
RNA, Fungal
Structure-Activity Relationship
RNA
A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Peptide Elongation Factor Tu
A protein found in bacteria and eukaryotic mitochondria which delivers aminoacyl-tRNA's to the A site of the ribosome. The aminoacyl-tRNA is first bound to a complex of elongation factor Tu containing a molecule of bound GTP. The resulting complex is then bound to the 70S initiation complex. Simultaneously the GTP is hydrolyzed and a Tu-GDP complex is released from the 70S ribosome. The Tu-GTP complex is regenerated from the Tu-GDP complex by the Ts elongation factor and GTP.
Magnesium
Yeasts
Base Pairing
Nitrogenous Group Transferases
Catalytic Domain
Genes, Suppressor
Alanine
Catalysis
Ribosomes
Ribonuclease T1
Codon
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).
Evolution, Molecular
RNA, Archaeal
Sequence Homology, Amino Acid
Biocatalysis
Peptide Elongation Factor 1
Peptide elongation factor 1 is a multisubunit protein that is responsible for the GTP-dependent binding of aminoacyl-tRNAs to eukaryotic ribosomes. The alpha subunit (EF-1alpha) binds aminoacyl-tRNA and transfers it to the ribosome in a process linked to GTP hydrolysis. The beta and delta subunits (EF-1beta, EF-1delta) are involved in exchanging GDP for GTP. The gamma subunit (EF-1gamma) is a structural component.
Mutagenesis, Site-Directed
Protein Structure, Tertiary
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Species Specificity
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Geobacillus stearothermophilus
Crystallography, X-Ray
Hydrogen Bonding
Suppression, Genetic
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).
Mitochondrial Diseases
Diseases caused by abnormal function of the MITOCHONDRIA. They may be caused by mutations, acquired or inherited, in mitochondrial DNA or in nuclear genes that code for mitochondrial components. They may also be the result of acquired mitochondria dysfunction due to adverse effects of drugs, infections, or other environmental causes.
Peptide Biosynthesis
The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.
Mitochondria
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Poly U
Peptide Elongation Factors
Protein Binding
Point Mutation
Methanococcus
Mutagenesis
Peptide Chain Elongation, Translational
RNA, Catalytic
RNA that has catalytic activity. The catalytic RNA sequence folds to form a complex surface that can function as an enzyme in reactions with itself and other molecules. It may function even in the absence of protein. There are numerous examples of RNA species that are acted upon by catalytic RNA, however the scope of this enzyme class is not limited to a particular type of substrate.
Chemistry
Tryptophan
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
Archaeoglobus fulgidus
Chemical Phenomena
Sequence Alignment
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Oligonucleotides
RNA Nucleotidyltransferases
Pyrophosphatases
Models, Chemical
Archaea
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
Cloning, Molecular
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Peptide Chain Initiation, Translational
A process of GENETIC TRANSLATION whereby the formation of a peptide chain is started. It includes assembly of the RIBOSOME components, the MESSENGER RNA coding for the polypeptide to be made, INITIATOR TRNA, and PEPTIDE INITIATION FACTORS; and placement of the first amino acid in the peptide chain. The details and components of this process are unique for prokaryotic protein biosynthesis and eukaryotic protein biosynthesis.
Nucleic Acid Denaturation
Disruption of the secondary structure of nucleic acids by heat, extreme pH or chemical treatment. Double strand DNA is "melted" by dissociation of the non-covalent hydrogen bonds and hydrophobic interactions. Denatured DNA appears to be a single-stranded flexible structure. The effects of denaturation on RNA are similar though less pronounced and largely reversible.
Threonine
Spermine
A biogenic polyamine formed from spermidine. It is found in a wide variety of organisms and tissues and is an essential growth factor in some bacteria. It is found as a polycation at all pH values. Spermine is associated with nucleic acids, particularly in viruses, and is thought to stabilize the helical structure.
Thermodynamics
A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
Electrophoresis, Polyacrylamide Gel
Adenosine
Deoxyribonucleotides
Chromatography
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
Plasmids
Cell-Free System
A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)
Serine
Transcription, Genetic
Conserved Sequence
Stereoisomerism
Macromolecular Substances
Cytoplasm
DNA, Mitochondrial
RNA-Binding Proteins
5'-Capping structures of Artemia salina mRNA and the translational inhibition by cap analogs. (1/111)
The mRNA of the brain shrimp Artemia salina has two types of blocked methylated 5'-terminal structures (caps). About 75% of the mRNA molecules have the 5'-end structure of m7G5'ppp5'-AmpGp and about 25% have the structure of m7G5'ppp5'GmpGp. The only other type of methylated residue found in Artemia mRNA is N6-methyladenosine and which is located at internal positions along the mRNA chain. Translation of Artemia cyst or nauplius poly(A)-rich mRNA in wheat-germ extracts was found to be inhibited by 7-methylguanosine 5'-monophosphate, a chemical analog of the cap, as well as by snythetic caps such as m7G5'ppp5'Gm. On the other hand, the elongation activity on endonegous mRNA in an Artemia cell-free system was not sensitive to 7-methylguanosine 5'-monophosphate. (+info)Translational step inhibited in vivo by aflatoxin B1 in rat-liver polysomes. (2/111)
Aflatoxin B1 strongly inhibits protein synthesis in rat liver cells. We previously demonstrated that this inhibition could be divided into two steps: up to 5 h aflatoxin blocks protein synthesis directly and specifically at the polysome level; beyond 7 h protein synthesis inhibition appears chiefly as a consequence of transcription impairment due to drug action. This paper confirms the foregoing results and represents an attempt to localize the translational step inhibited in vivo by aflatoxin B1. We used the simulation study developed by Li, Kisilevsky, Wasan and Hammond, 1972 (Biochim. Biophys. Acta, 272, 451-462) to determine precisely the site inhibited in vivo after drug intoxication. This analysis is based on two parameters: the kinetics of polysome labeling to follow the nascent peptide synthesis, and the kinetics of supernatant labeling to follow the completed protein synthesis. Up to 5 h after dosing, aflatoxin specifically inhibits the elongation and/or termination steps during protein synthesis; after longer periods of time inhibition occurs essentially at the initiation step. When the intracellular concentration of aflatoxin is too high, particularly 2 h after dosing, each step of protein synthesis is blocked. Polypeptide synthesis by the postmitochondrial supernatants isolated from aflatoxin-treated animals is impaired in the same proportion as protein synthesis in vivo. The damage caused by aflatoxin is mostly observed on microsomes. However, purified polysomes isolated from aflatoxin-treated rats synthesize proteins in vitro to the same extent as those from controls. These results suggest that aflatoxin metabolite(s) are bound to polysomes with noncovalent bonds. These active metabolites are probably lost during polysome isolation procedures. Finally, relationships between protein metabolism and aflatoxin carcinogenesis are discussed. (+info)Polyanion-induced release of polyribosomes from HeLa cell nuclei. (3/111)
Intact detergent-washed HeLa nuclei contain a population of polyribisomes that were released by exposure to polyanions such as RNA or poly(U). The released material appeared by electron microscopic examination to be particles averaging about 200 to 300 angstroms in diameter. Sedimentation velocity analysis of the released particles indicated that the particles had S20,w values of 75 and 110. The particles stimulated amino acid incorporation in an ascites S-30 or S-100 extract at 2.5 mM Mg2+. Studies with a variety of antibiotics indicated that these polyribosomes were capable of elongating but not initiating protein synthesis. Although these polyribosomes may be of cytoplasmic origin, they appear unique in that agents thought to disperse chromatin are required for their release from the nucleus. (+info)Properties of biologically active messenger RNA from human placenta. Cell-free synthesis of two immunoreactive forms of placental lactogen. (4/111)
In order to understand better the regulation of human placental proteins the activity of placental lactogen messenger RNA has been examined. Total RNA was extracted from normal term placentas and purified by chromatography on oligo(dT)-cellulose. The poly(A)-containing fraction stimulated amino acid incorporation 5- to 10-fold in wheat germ cell-free extracts, and immunoprecipitation of the translation products with antiserum directed against human placental lactogen (hPL) suggests that about 2% of the peptides contain hPL determinants. Analysis of the material precipitated with hPL antiserum by electrophoresis on sodium dodecyl sulfate-polyacrylamide gels revealed two major species, one co-migrating with hPL and the other migrating slightly slower than hPL. On DEAE-cellulose chromatography the former material eluted close to authentic hPL while the latter material eluted at higher ionic strength than hPL, indicating a difference in net charge of these two species. Tryptic peptide analysis of the large material and authentic hPL shows marked similarities in the primary structure of these two proteins. The slower migrating peptide has an apparent molecular weight about 3000 larger than hPL and thus may represent a precursor molecule. Both cell-free products could be competed out of immunoprecipitates by a large excess of authentic hPL, confirming their immunologic similarities. Centrifugation of the placental poly(A)-containing RNA through aqueous glycerol gradients indicates that the hPL mRNA sediments at about 14 S. (+info)(De)regulation of key enzyme steps in the shikimate pathway and phenylalanine-specific pathway of the actinomycete Amycolatopsis methanolica. (5/111)
Prephenate dehydratase (PDT), chorismate mutase (CM) and 3-deoxy-D-arabino-7-heptulosonate 7-phosphate (DAHP) synthase are key regulatory enzymes in aromatic amino acid biosynthesis in the actinomycete Amycolatopsis methanolica. Deregulated, feedback-control-resistant mutants were isolated by incubation of A. methanolica on glucose mineral agar containing the toxic analogue p-fluoro-DL-phenylalanine (pFPhe). Several of these mutants had completely lost PDT sensitivity to Phe inhibition and Tyr activation. Mutant characterization yielded new information about PDT amino acid residues involved in Phe and Tyr effector binding sites. A. methanolica wild-type cells grown on glucose mineral medium normally possess a bifunctional CM/DAHP synthase protein complex (with DS1, a plant-type DAHP synthase). The CM activity of this protein complex is feedback-inhibited by Tyr and Phe, while DS1 activity is mainly inhibited by Trp. Isolation of pFPhe-resistant mutants yielded two feedback-inhibition-resistant CM mutants. These were characterized as regulatory mutants, derepressed in (a) synthesis of CM, now occurring as an abundant, feedback-inhibition-resistant, separate protein, and (b) synthesis of an alternative DAHP synthase (DS2, an E. coli-type DAHP synthase), only inhibited by Tyr and Trp. DS1 and DS2 thus are well integrated in A. methanolica primary metabolism: DS1 and CM form a protein complex, which stimulates CM activity and renders it sensitive to feedback inhibition by Phe and Tyr. Synthesis of CM and DS2 proteins appears to be controlled co-ordinately, sensitive to Phe-mediated feedback repression. (+info)Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution. (6/111)
The fidelity of aminoacylation of tRNA(Thr) by the threonyl-tRNA synthetase (ThrRS) requires the discrimination of the cognate substrate threonine from the noncognate serine. Misacylation by serine is corrected in a proofreading or editing step. An editing site has been located 39 A away from the aminoacylation site. We report the crystal structures of this editing domain in its apo form and in complex with the serine product, and with two nonhydrolyzable analogs of potential substrates: the terminal tRNA adenosine charged with serine, and seryl adenylate. The structures show how serine is recognized, and threonine rejected, and provide the structural basis for the editing mechanism, a water-mediated hydrolysis of the mischarged tRNA. When the adenylate analog binds in the editing site, a phosphate oxygen takes the place of one of the catalytic water molecules, thereby blocking the reaction. This rules out a correction mechanism that would occur before the binding of the amino acid on the tRNA. (+info)Comparative analysis of the pathogenic mechanisms associated with the G8363A and A8296G mutations in the mitochondrial tRNA(Lys) gene. (7/111)
Two mutations (G8363A and A8296G) in the mtDNA (mitochondrial DNA) tRNA(Lys) gene have been associated with severe mitochondrial diseases in a number of reports. Their functional significance, however, remains unknown. We have already shown that homoplasmic cybrids harbouring the A8296G mutation display normal oxidative phosphorylation, although the possibility of a subtle change in mitochondrial respiratory capacity remains an open issue. We have now investigated the pathogenic mechanism of another mutation in the tRNA(Lys) gene (G8363A) by repopulating an mtDNA-less human osteosarcoma cell line with mitochondria harbouring either this genetic variant alone or an unusual combination of the two mutations (A8296G+G8363A). Cybrids homoplasmic for the single G8363A or the A8296G+G8363A mutations have defective respiratory-chain enzyme activities and low oxygen consumption, indicating a severe impairment of the oxidative phosphorylation system. Generation of G8363A cybrids within a wild-type or the A8296G mtDNA genetic backgrounds resulted in an important alteration in the conformation of the tRNA(Lys), not affecting tRNA steady-state levels. Moreover, mutant cybrids have an important decrease in the proportion of amino-acylated tRNA(Lys) and, consequently, mitochondrial protein synthesis is greatly decreased. Our results demonstrate that the pathogenicity of the G8363A mutation is due to a change in the conformation of the tRNA that severely impairs aminoacylation in the absence of changes in tRNA stability. The only effect detected in the A8296G mutation is a moderate decrease in the aminoacylation capacity, which does not affect mitochondrial protein biosynthesis. (+info)Divergent anticodon recognition in contrasting glutamyl-tRNA synthetases. (8/111)
The pathogenic bacterium Helicobacter pylori utilizes two essential glutamyl-tRNA synthetases (GluRS1 and GluRS2). These two enzymes are closely related in evolution and yet they aminoacylate contrasting tRNAs. GluRS1 is a canonical discriminating GluRS (D-GluRS) that biosynthesizes Glu-tRNA(Glu) and cannot make Glu-tRNA(Gln). In contrast, GluRS2 is non-canonical as it is only essential for the production of misacylated Glu-tRNA(Gln). The co-existence and evident divergence of these two enzymes was capitalized upon to directly examine how GluRS2 acquired tRNA(Gln) specificity. One key feature that distinguishes tRNA(Glu) from tRNA(Gln) is the third position in the anticodon of each tRNA (C36 versus G36, respectively). By comparing sequence alignments of different GluRSs, including GluRS1s and GluRS2s, to the crystal structure of the Thermus thermophilus D-GluRS:tRNA(Glu) complex, a divergent pattern of conservation in enzymes that aminoacylate tRNA(Glu)versus those specific for tRNA(Gln) emerged and was experimentally validated. In particular, when an arginine conserved in discriminating GluRSs and GluRS1s was inserted into Hp GluRS2 (Glu334Arg GluRS2), the catalytic efficiency of the mutant enzyme (k(cat)/K(Mapp)) was reduced by approximately one order of magnitude towards tRNA(Gln). However, this mutation did not introduce activity towards tRNA(Glu). In contrast, disruption of a glycine that is conserved in all GluRS2s but not in other GluRSs (Gly417Thr GluRS2) generated a mutant GluRS2 with weak activity towards tRNA(Glu1). Synergy between these two mutations was observed in the double mutant (Glu334Arg/Gly417Thr GluRS2), which specifically and more robustly aminoacylates tRNA(Glu1) instead of tRNA(Gln). As GluRS1 and GluRS2 are related by an apparent gene duplication event, these results demonstrate that we can experimentally map critical evolutionary events in the emergence of new tRNA specificities. (+info)Cellular mechanisms that control mistranslation | Meta
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Catherine Jivora
Aminoacylation
... is the process of adding an aminoacyl group to a compound. Acylation tRNA aminoacylation Transfer RNA-like ... structures Jafarnejad, Seyed Mehdi; Kim, Sung-Hoon; Sonenberg, Nahum (9 January 2018). "Aminoacylation of Proteins: New Targets ...
Hypercycle (chemistry)
A transaminoacylator described in 2013 has five nucleotides, which is sufficient for a trans-amino acylation reaction and makes ... "Ribozyme-catalyzed tRNA aminoacylation". Nature Structural Biology. 7 (1): 28-33. doi:10.1038/71225. PMID 10625423. S2CID ...
Paul Schimmel
Francklyn, C.; Shi, J. P.; Schimmel, P. (1992-02-28). "Overlapping nucleotide determinants for specific aminoacylation of RNA ... Francklyn, C.; Schimmel, P. (1989-02-02). "Aminoacylation of RNA minihelices with alanine". Nature. 337 (6206): 478-481. doi: ...
Amino acid activation
Swanson R, Hoben P, Sumner-Smith M, Uemura H, Watson L, Söll D (December 1988). "Accuracy of in vivo aminoacylation requires ... Amino acid activation (also known as aminoacylation or tRNA charging) refers to the attachment of an amino acid to its ... Pang YL, Poruri K, Martinis SA (2014). "tRNA synthetase: tRNA aminoacylation and beyond". Wiley Interdisciplinary Reviews. 5 (4 ...
Tyrosine-tRNA ligase
These latter enzymes link amino acids to their cognate transfer RNAs (tRNA) in aminoacylation reactions that establish the ... Bonnefond L, Giegé R, Rudinger-Thirion J (Sep 2005). "Evolution of the tRNA(Tyr)/TyrRS aminoacylation systems". Biochimie. 87 ( ... the first step of the aminoacylation reaction) and for transferring the amino-acid moiety from tyrosyl-adenylate to the 3'OH- ... CCA terminus of the cognate tRNA(Tyr) (the second step of the aminoacylation reaction). The other domains are responsible (i) ...
Transfer RNA-like structures
tRNA-like structures mimic some tRNA function, such as aminoacylation. There are three aminoacylation specificities, valine, ...
Diabetes and deafness
... structure also results in decreased aminoacylation. The mutation has also been shown to result in decreased function of the ...
William H. McClain
"The selective tRNA aminoacylation mechanism based on a single G•U pair". Nature. 510 (7506): 507-511. Bibcode:2014Natur.510.. ... "The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation". Proceedings of the National Academy ... importance of tRNA backbone-mediated interactions with synthetase in mediating molecular recognition conferring aminoacylation ...
RARS (gene)
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in ... "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase". The Journal of Biological Chemistry ...
Kinetic proofreading
Hopfield JJ, Yamane T, Yue V, Coutts SM (April 1976). "Direct experimental evidence for kinetic proofreading in amino acylation ...
Aminoacyl tRNA synthetases, class I
Perona JJ, Steitz TA, Rould MA (1993). "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA ...
Ribozyme
Metal Ion Requirements in Artificial Ribozymes that Catalyze Aminoacylation and Redox Reactions". Metal ion requirements in ... artificial ribozymes that catalyze aminoacylation and redox reactions. Metal Ions in Life Sciences. Vol. 9. pp. 277-97. doi: ...
Transfer RNA
Aminoacylation is the process of adding an aminoacyl group to a compound. It covalently links an amino acid to the CCA 3′ end ... Interference with aminoacylation may be useful as an approach to treating some diseases: cancerous cells may be relatively ... Hence, inhibition of aminoacylation of specific tRNA species is considered a promising novel avenue for the rational treatment ... vulnerable to disturbed aminoacylation compared to healthy cells. The protein synthesis associated with cancer and viral ...
YARS
Wakasugi K, Quinn CL, Tao N, Schimmel P (1998). "Genetic code in evolution: switching species-specific aminoacylation with a ... Aminoacyl-tRNA synthetases catalyze the aminoacylation of transfer RNA (tRNA) by their cognate amino acid. Because of their ...
SCYE1
1999). "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase". J. Biol. Chem. 274 (24): ...
Glycine-tRNA ligase
Hipps D, Shiba K, Henderson B, Schimmel P (Jun 1995). "Operational RNA code for amino acids: species-specific aminoacylation of ... Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation". The Journal of Biological ...
Aminoacyl tRNA synthetases, class II
Perona JJ, Steitz TA, Rould MA (1993). "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA ...
VARS
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in ...
WARS2
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in ...
Expanded genetic code
Thus far, this system has only been shown to work in an in-vitro translation setting where the aminoacylation of the orthogonal ... Ohuchi M, Murakami H, Suga H (October 2007). "The flexizyme system: a highly flexible tRNA aminoacylation tool for the ...
IARS
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in ...
2-Aminoisobutyric acid
Ohuchi, Masaki; Murakami, Hiroshi; Suga, Hiroaki (2007). "The flexizyme system: a highly flexible tRNA aminoacylation tool for ...
TARS (gene)
Aminoacyl tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in ...
QARS
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in ...
Aminoacyl-tRNA
Swanson R, Hoben P, Sumner-Smith M, Uemura H, Watson L, Söll D (December 1988). "Accuracy of in vivo aminoacylation requires ... It is thermodynamically favorable that the aminoacylation process yield a stable aa-tRNA molecule, thus providing for the ...
Aminoacyl tRNA synthetase
Swanson R, Hoben P, Sumner-Smith M, Uemura H, Watson L, Söll D (December 1988). "Accuracy of in vivo aminoacylation requires ...
Susan A. Martinis
Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase., Nat. Struct. ... "Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase". Nature ...
Transfer-messenger RNA
Functional evidence, i.e., mt-tmRNA Aminoacylation with alanine, is available for Jakoba libera. More recently, ssrA was also ... including the acceptor stem with elements like those in alanine tRNA that promote its aminoacylation by alanine-tRNA ligase. It ...
LARS2
Each of the twenty aminoacyl-tRNA synthetases catalyzes the aminoacylation of a specific tRNA or tRNA isoaccepting family with ... decreases the efficiency of aminoacylation". Biochemistry. 42 (4): 958-64. doi:10.1021/bi026882r. PMID 12549915. Yao YN, Wang L ...
Leucyl-tRNA synthetase
"A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation". Biochemistry. 46 (15): ...
IMSEAR at SEARO: Influence of monovalent cations on aminoacylation of transfer RNA.
Network Portal - Function mitochondrial lysyl-tRNA aminoacylation
Glu-Q-tRNA(Asp) synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNA(Asp)...
The Origin of Life
Protein synthesis requires the aminoacylation of RNA, and it is in this step that L-amino acids could have been selected for, ... Tamura K, Schimmel P (2004) Chiral-selective aminoacylation of an RNA minihelix. Science 305:1253 [Pubmed] ... Tamura K, Schimmel P (2006) Chiral-selective aminoacylation of an RNA minihelix: Mechanistic features and chiral suppression. ...
Protein translation, steroide kaufen ohne zoll anabolika kur wie lange | Profil
MT-TS1 gene: MedlinePlus Genetics
Jack Szostak | Harvard Catalyst Profiles | Harvard Catalyst
SMART: Arg tRNA synt N domain annotation
Leucine-rich diet alters the eukaryotic translation initiation factors expression in skeletal muscle of tumour-bearing rats |...
YRC Public Data Repository - Protein Overview - SES1 / YDR023W
Triple-negative breast cancer cells respond to T cells severely at the alternative splicing layer | Zhao | Electronic Journal...
Gene rearrangements in gekkonid mitochondrial genomes with shuffling, loss, and reassignment of tRNA genes | BMC Genomics |...
Identification of Candidate Genes Associated with Charcot-Marie-Tooth Disease by Network and Pathway Analysis
... tRNA aminoacylation for protein translation, tRNA aminoacylation, and tRNA metabolic process). ... In addition, terms such as ensheathment of neurons, axon ensheathment, myelination, tRNA aminoacylation for protein translation ... The main mechanisms proposed consist of reduction of aminoacylation activity, alteration of dimerization or localization, ... peripheral nervous system development, tRNA aminoacylation, amino acid activation, selective autophagy, Schwann cell ...
Research: Prof. Dr. Beat Suter - Institute of Cell Biology
Ho, Manh Tin; Lu, Jiongming; Brunssen, Dominique Yvonne; Suter, Beat (2021). An aminoacylation independent activity of PheRS/ ... In order to assess the importance of aminoacylation fidelity in multicellular organisms, we generated an amino-acid double- ... Interestingly, many aaRSs also perform additional functions in the cell, unrelated to their aminoacylation function. It is ...
IJMS | Special Issue : Protein Synthesis and Disease
6pom - Proteopedia, life in 3D
T-boxes directly bind tRNAs, assess their aminoacylation state, and regulate the transcription or translation of downstream ... In the absence of aminoacylation, T-boxes clutch tRNAs and form a continuously stacked central spine, permitting ... and interrogates its aminoacylation state using a steric filter fashioned from a wobble base pair. ...
MH DELETED MN ADDED MN
Solyc07g020710.3.1 details
Patrick Pierre Lestienne - CV - Director of Research INSERM
Arginyl-tRNA synthetase, mitochondrial (P38714) - Yeast Metabolome Database
Mehanizam diskriminacije leucina u mjestu za popravak pogreške leucil-tRNA-sintetaze | Repository of Faculty of Science
DeCS 2005 - Deleted terms
DeCS 2005 - Deleted terms
DeCS 2005 - Deleted terms
DeCS 2005 - Deleted terms
DeCS 2005 - Deleted terms
DeCS 2005 - Deleted terms
DeCS
Amino Acylation. Amino Acylations. Aminoacylations. Tree number(s):. G02.111.012.055. G02.111.660.050. G02.607.063.526. G03.040 ... Aminoacylation - Preferred Concept UI. M0463735. Scope note. A reaction that introduces an aminoacyl group to a molecule. ... TRANSFER RNA AMINOACYLATION is the first step in GENETIC TRANSLATION.. Annotation:. not for activation of enzymes, receptors, ... Aminoacylation Entry term(s):. Acids Activation, Amino. Acids Activations, Amino. Activation of Amino Acids. Acylation, Amino. ...
TRNATranslationActivationTransferArginyl-tRNAMitochondrialSynthetasePhenylalanyl-tRNA aminoacylationAcceptor stemEffects on aminoacylationCatalyzes the aminoacylationSpecific aminoacylationTRNAsPathwaysBiologicalNucleotideCognateSpecificityAlaRSEfficientAnticodonAmino acidsModificationStructuralCrucialSecondaryDevelopmentFunctionSenseDomains
TRNA13
- In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. (systemsbiology.net)
- The functional properties of YadB contrast with those of the canonical glutamyl-tRNA synthetases, which activate Glu only in presence of the cognate tRNA before aminoacylation of the 3'-end of tRNA. (nih.gov)
- Biological pathway analyses showed that translation initiation and tRNA aminoacylation pathways were most disturbed with T cell treatment. (ejbiotechnology.info)
- The T-box forms a U-shaped molecular vise that clamps the tRNA, captures its 3' end using an elaborate 'discriminator' structure, and interrogates its aminoacylation state using a steric filter fashioned from a wobble base pair. (proteopedia.org)
- The model has so far been applied on 998 prokaryotic genomes, and results include ~400000 specific annotations with the estimated Precision of 90%, ~19000 of which are highly specific-e.g. "penicillin binding," "tRNA aminoacylation for protein translation," or "pathogenesis"-and are freely available at http://gorbi.irb.hr/ . (irb.hr)
- Aspartyl-tRNA synthetase catalyzes the attachment of aspartic acid to its cognate tRNA by the aminoacylation reaction during the initiation of the protein biosynthesis process. (bvsalud.org)
- In the second step of the aminoacylation reaction, known as the charging step, the aspartate moiety is transferred from aspartyl-adenylate to the 3'-OH of A76 of tRNA through a proton transfer process. (bvsalud.org)
- This process is highly dependent on the fidelity of tRNA aminoacylation by aminoacyl-tRNA synthetases and relies primarily on sets of identities within tRNA molecules composed of determinants and antideterminants preventing mischarging by non-cognate synthetases. (bvsalud.org)
- Since then, the panel of identity elements governing the accuracy of tRNA aminoacylation has expanded considerably, but the increasing number of reported functional idiosyncrasies has led to some confusion. (bvsalud.org)
- In parallel, the description of other processes involving tRNAs, often well beyond aminoacylation, has progressed considerably, greatly expanding their interactome and uncovering multiple novel identities on the same tRNA molecule. (bvsalud.org)
- The tRNA molecules, in addition to translating the genetic code into protein and defining the second genetic code via their aminoacylation by aminoacyl-tRNA synthetases, act in many other cellular functions and dysfunctions. (cnrs.fr)
- Determining the fidelity of tRNA aminoacylation via microarrays. (uchicago.edu)
- Cross-species aminoacylation experiments showed that threonyl-tRNA synthetase from A. pernix threonylated not only Escherichia coli threonine tRNA having A73 as a discriminator base, but also an extreme halophilic archaeon Haloferax volcanii threonine tRNA possessing U73. (archive.org)
Translation3
- T-boxes directly bind tRNAs, assess their aminoacylation state, and regulate the transcription or translation of downstream genes to maintain nutritional homeostasis. (proteopedia.org)
- In the absence of aminoacylation, T-boxes clutch tRNAs and form a continuously stacked central spine, permitting transcriptional readthrough or translation initiation. (proteopedia.org)
- TRANSFER RNA AMINOACYLATION is the first step in GENETIC TRANSLATION . (bvsalud.org)
Activation1
- The aminoacylation response usually starts using the activation of proteins to create aminoacyl-adenosine monophosphate (AMP), accompanied by the charging of tRNA8. (bioinf.org)
Transfer1
- IMSEAR at SEARO: Influence of monovalent cations on aminoacylation of transfer RNA. (who.int)
Arginyl-tRNA1
- Nevertheless, the deletion from the C-terminus of hcLeuRS didn't influence the aminoacylation activity, but affected its discussion with arginyl-tRNA synthetase in the mammalian macromolecular complicated (42). (cp-724714.com)
Mitochondrial3
- Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation. (cas.cn)
- Hearing impairment-associated KARS mutations lead to defects in aminoacylation of both cytoplasmic and mitochondrial tRNA Lys . (cas.cn)
- They found that in the fibroblasts, the vital step for correct mitochondrial protein synthesis catalyzed by GatCAB - aminoacylation of glutamyl tRNA - was perturbed, thus affecting the levels of the amino acid glutamine (the amino acid specific to glutamyl tRNA). (mitochondrialdiseasenews.com)
Synthetase4
- 12. Human tryptophanyl-tRNA synthetase binds with heme to enhance its aminoacylation activity. (nih.gov)
- A single non-Watson-Crick base pair in the tRNA for alanine, G3·U70, ensures correct aminoacylation by the synthetase (AlaRS). (natureasia.com)
- EPRS is a bifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species. (ptglab.com)
- However, the aminoacylation of tRNA(Ile2) by methionyl-tRNA synthetase (MetRS), before the modification by TilS, might lead to the misincorporation of methionine in response to isoleucine codons. (survivinpathway.com)
Phenylalanyl-tRNA aminoacylation1
- Predicted to be involved in phenylalanyl-tRNA aminoacylation. (nih.gov)
Acceptor stem4
- However, the anticodon stem-loop microhelix did not enhance aminoacylation of the acceptor stem microhelix. (illinois.edu)
- Efficient aminoacylation of the tRNA(Ala) acceptor stem: dependence on the 2:71 base pair. (irbbarcelona.org)
- tRNALeu, its amino acidity acceptor stem as well as the elbow area at the part of L-shaped tRNA make immediate connections with LeuRS and so are named two important models for aminoacylation and editing and enhancing (16C20). (cp-724714.com)
- For example, almost all known alanine tRNA (tRNAAla) isoacceptors contain a G3:U70 wobble base pair in the acceptor stem that identifies tRNAAla for aminoacylation with alanine. (ncu.edu.tw)
Effects on aminoacylation1
- This has been exploited in a systematic analysis of the effects on aminoacylation of nine pathology-related mutations described so far. (nih.gov)
Catalyzes the aminoacylation1
- WARS catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by INF. (prospecbio.com)
Specific aminoacylation2
- This mechanism explains how a small number of nucleotides distant from the catalytic site can determine the reactivity of specific aminoacylation. (natureasia.com)
- Maturation of tRNA to a functional RNA requires processing of the extensional sequences and post-transcriptional chemical modifications, which ensures the specific aminoacylation of tRNA by the cognate aaRS. (elsevier.com)
TRNAs4
- One step that's crucial is aminoacylation, the attachment of amino acids to their proper tRNAs. (nih.gov)
- Remarkably, the T-boxes directly sense the aminoacylation states of bound tRNAs to gauge intracellular amino acid availability, and direct a transcriptional or translational switch to regulate amino acid biosynthesis, transport, and tRNA aminoacylation. (nih.gov)
- It is increasingly clear that the aminoacylation state of tRNAs can serve as crucial indicators of overall cellular well-being in both bacteria and eukaryotes. (nih.gov)
- For efficient aminoacylation, tRNAs carry the conserved 3'-terminal sequence C-C-A, which is synthesized by highly specific tRNA nucleotidyltransferases (CCA-adding enzymes). (omicsdi.org)
Pathways1
- Biological pathway analyses showed that translation initiation and tRNA aminoacylation pathways were most disturbed with T cell treatment. (bvsalud.org)
Biological1
- Dr. Paul R. Schimmel and his team at The Scripps Research Institute conducted a series of molecular studies and deciphered a high-resolution chemical structure that reveals how the compound jams the process of aminoacylation, a crucial biological process that allows organisms to synthesize the proteins they require to live. (nih.gov)
Nucleotide1
- Identification from the elbow area is very important to effective leucylation because nucleotide mutations within this domains distorted tRNALeu orientation and impacted upon aminoacylation and editing reactions (19). (cp-724714.com)
Cognate1
- Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. (antikoerper-online.de)
Specificity1
- 2'- Versus 3'-OH specificity in tRNA aminoacylation. (elsevier.com)
AlaRS1
- CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS. (uchicago.edu)
Efficient1
- Thus, transduction of the anticodon identity signal may require covalent continuity of the tRNA chain to trigger efficient aminoacylation. (illinois.edu)
Anticodon1
- Our data show that the tRNACAG(Ser) emerged from insertion of an adenosine in the middle position of the 5'-CGA-3'anticodon of a tRNACGA(Ser) ancestor, producing the 5'-CAG-3' anticodon of the tRNACAG(Ser), without altering its aminoacylation properties. (nih.gov)
Amino acids1
- In the November 26, 2009, issue of Nature , the team described a new method that can measure the accuracy of aminoacylation for 6 of the 20 amino acids. (nih.gov)
Modification1
- Laurino, P.* Evolutionary repair reveals an unexpected role of the tRNA modification m1G37 in aminoacylation. (oist.jp)
Structural1
- Battaglia, R. A. , Grigg, J. C. , and Ke, A. (2019) Structural basis for tRNA decoding and aminoacylation sensing by T-box riboregulators . (cornell.edu)
Crucial1
- Today's work exposed a crucial part from the bacterial LeuRS-CTD in tRNA binding and its own reputation in both aminoacylation and editing. (cp-724714.com)
Secondary1
- The sole mutation located in a loop of the tRNA secondary structure, A8344G, does not affect aminoacylation efficiency. (nih.gov)
Development2
- Potential for interdependent development of tRNA determinants for aminoacylation and ribosome decoding. (jefferson.edu)
- Interestingly, three independent forward-genetic studies in zebrafish showed a role for SerRS in vascular development that is independent of aminoacylation ( 2-4 ). (stanford.edu)
Function1
- Mutational research on the tRNA 3-CCA76 end uncovered its function in orientating the CP1 domains in accordance with the LeuRS artificial domains in aminoacylation. (cp-724714.com)
Sense1
- The antiterminator domain detects the molecular volume of the tRNA 3' end to sense aminoacylation. (nih.gov)
Domains2
- Out of eight mutations located in helical domains converting canonical Watson-Crick pairs into G-U pairs or C.A mismatches, six have no effect on aminoacylation (A8296G, U8316C, G8342A, U8356C, U8362G, G8363A), and two lead to drastic decreases (5000- to 7000-fold) in lysylation efficiencies (G8313A and G8328A). (nih.gov)
- As the tree of life was ascended, tRNA synthetases added new domains, which are generally dispensable for aminoacylation, in a progressive and accretive manner. (stanford.edu)