Caenorhabditis elegans: A species of nematode that is widely used in biological, biochemical, and genetic studies.Caenorhabditis elegans Proteins: Proteins from the nematode species CAENORHABDITIS ELEGANS. The proteins from this species are the subject of scientific interest in the area of multicellular organism MORPHOGENESIS.Caenorhabditis: A genus of small free-living nematodes. Two species, CAENORHABDITIS ELEGANS and C. briggsae are much used in studies of genetics, development, aging, muscle chemistry, and neuroanatomy.Genes, Helminth: The functional hereditary units of HELMINTHS.Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.Algorithms: A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.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.Helminth Proteins: Proteins found in any species of helminth.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.RNA, Transfer, Amino Acyl: 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.Elongation Factor 2 Kinase: A monomeric calcium-calmodulin-dependent protein kinase subtype that specifically phosphorylates PEPTIDE ELONGATION FACTOR 2. The enzyme lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE, however it is regulated by phosphorylation by PROTEIN KINASE A and through intramolecular autophosphorylation.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.Peptide Elongation Factor 2: Peptide Elongation Factor 2 catalyzes the translocation of peptidyl-tRNA from the A site to the P site of eukaryotic ribosomes by a process linked to the hydrolysis of GTP to GDP.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.Isoleucine-tRNA Ligase: An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.Peptide Elongation Factors: Protein factors uniquely required during the elongation phase of protein synthesis.Dictionaries, MedicalTransfer RNA Aminoacylation: The conversion of uncharged TRANSFER RNA to AMINO ACYL TRNA.Methionine-tRNA Ligase: An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10.Lysine-tRNA Ligase: An enzyme that activates lysine with its specific transfer RNA. EC 6.1.1.6.Glutamate-tRNA Ligase: An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.Dictionaries as Topic: Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.Leucine-tRNA Ligase: An enzyme that activates leucine with its specific transfer RNA. EC 6.1.1.4.Aminoacylation: A reaction that introduces an aminoacyl group to a molecule. TRANSFER RNA AMINOACYLATION is the first step in GENETIC TRANSLATION.Peer Review: An organized procedure carried out by a select committee of professionals in evaluating the performance of other professionals in meeting the standards of their specialty. Review by peers is used by editors in the evaluation of articles and other papers submitted for publication. Peer review is used also in the evaluation of grant applications. It is applied also in evaluating the quality of health care provided to patients.Peer Review, Research: The evaluation by experts of the quality and pertinence of research or research proposals of other experts in the same field. Peer review is used by editors in deciding which submissions warrant publication, by granting agencies to determine which proposals should be funded, and by academic institutions in tenure decisions.Publishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.History, 19th Century: Time period from 1801 through 1900 of the common era.Bibliometrics: The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)Periodicals as Topic: A publication issued at stated, more or less regular, intervals.History, 20th Century: Time period from 1901 through 2000 of the common era.Publications: Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)Editorial Policies: The guidelines and policy statements set forth by the editor(s) or editorial board of a publication.Research: Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)

In vivo and in vitro processing of the Bacillus subtilis transcript coding for glutamyl-tRNA synthetase, serine acetyltransferase, and cysteinyl-tRNA synthetase. (1/1309)

In Bacillus subtilis, the adjacent genes gltX, cysE, and cysS encoding respectively glutamyl-tRNA synthetase, serine acetyl-transferase, and cysteinyl-tRNA synthetase, are transcribed as an operon but a gltX probe reveals only the presence of a monocistronic gltX mRNA (Gagnon et al., 1994, J Biol Chem 269:7473-7482). The transcript of the gltX-cysE intergenic region contains putative alternative secondary structures forming a p-independent terminator or an antiterminator, and a conserved sequence (T-box) found in the leader of most aminoacyl-tRNA synthetase and many amino acid biosynthesis genes in B. subtilis and in other Gram-positive eubacteria. The transcription of these genes is initiated 45 nt upstream from the first codon of gltX and is under the control of a sigmaA-type promoter. Analysis of the in vivo transcript of this operon revealed a cleavage site immediately downstream from the p-independent terminator structure. In vitro transcription analysis, using RNA polymerases from Escherichia coli, B. subtilis, and that encoded by the T7 phage, in the presence of various RNase inhibitors, shows the same cleavage. This processing generates mRNAs whose 5'-end half-lives differ by a factor of 2 in rich medium, and leaves putative secondary structures at the 3' end of the gltX transcript and at the 5' end of the cysE/S mRNA, which may be involved in the stabilization of these mRNAs. By its mechanism and its position, this cleavage differs from that of the other known transcripts encoding aminoacyl-tRNA synthetases in B. subtilis.  (+info)

The peculiar architectural framework of tRNASec is fully recognized by yeast AspRS. (2/1309)

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)

Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex. (3/1309)

Cytoplasmic aminoacyl-tRNA synthetases of higher eukaryotes acquired extra peptides in the course of their evolution. It has been thought that these appendices are related to the occurrence of the multiprotein complex consisting of at least eight different tRNA synthetase polypeptides. This complex is believed to be a signature feature of metazoans. In this study, we used multiple sequence alignments to infer the locations of the peptide appendices from human cytoplasmic tRNA synthetases found in the multisynthetase complex. The selected peptide appendices ranged from 22 aa of aspartyl-tRNA synthetase to 267 aa of methionyl-tRNA synthetase. We then made genetic constructions to investigate interactions between all 64 combinations of these peptides that were individually fused to nonsynthetase test proteins. The analyses identified 11 (10 heterologous and 1 homologous) interactions. The six peptide-dependent interactions paralleled what had been detected by crosslinking methods applied to the isolated multisynthetase complex. Thus, small peptide appendices seem to link together different synthetases into a complex. In addition, five interacting pairs that had not been detected previously were suggested from the observed peptide-dependent complexes.  (+info)

Immunoelectron microscopic localization of glutamyl-/ prolyl-tRNA synthetase within the eukaryotic multisynthetase complex. (4/1309)

A high molecular mass complex of aminoacyl-tRNA synthetases is readily isolated from a variety of eukaryotes. Although its composition is well characterized, knowledge of its structure and organization is still quite limited. This study uses antibodies directed against prolyl-tRNA synthetase for immunoelectron microscopic localization of the bifunctional glutamyl-/prolyl-tRNA synthetase. This is the first visualization of a specific site within the multisynthetase complex. Images of immunocomplexes are presented in the characteristic views of negatively stained multisynthetase complex from rabbit reticulocytes. As described in terms of a three domain working model of the structure, in "front" views of the particle and "intermediate" views, the primary antibody binding site is near the intersection between the "base" and one "arm." In "side" views, where the particle is rotated about its long axis, the binding site is near the midpoint. "Top" and "bottom" views, which appear as square projections, are also consistent with the central location of the binding site. These data place the glutamyl-/prolyl-tRNA synthetase polypeptide in a defined area of the particle, which encompasses portions of two domains, yet is consistent with the previous structural model.  (+info)

Ultrastructure of the eukaryotic aminoacyl-tRNA synthetase complex derived from two dimensional averaging and classification of negatively stained electron microscopic images. (5/1309)

Several aminoacyl-tRNA synthetases in higher eukaryotes are consistently isolated as a multi-enzyme complex for which little structural information is yet known. This study uses computational methods for analysis of electron microscopic images of the particle. A data set of almost 2000 negatively stained images was processed through reference-free alignment and multivariate statistical analysis. Interpretable structural information was evident in five eigenvectors. Hierarchical ascendant classification extracted clusters corresponding to distinct image orientations. The class averages are consistent with rotations around and orthogonal to a central particle axis and provide particle measurements: approximately 25 nm in height, 30 nm at the widest point and 23 nm thick. The results also provide objective evidence in support of the working structural model and demonstrate the feasibility of obtaining the three dimensional structure of the multisynthetase complex by single particle reconstruction methods.  (+info)

The identity determinants required for the discrimination between tRNAGlu and tRNAAsp by glutamyl-tRNA synthetase from Escherichia coli. (6/1309)

We previously elucidated the major determinant set for Escherichia coli tRNAGlu identity (U34, U35, C36, A37, G1*C72, U2*A71, U11*A24, U13*G22**Alpha46, and Delta47) and showed that the set is sufficient to switch the identity of tRNAGln to Glu [Sekine, S., Nureki, O., Sakamoto, K., Niimi, T., Tateno, M., Go, M., Kohno, T., Brisson, A., Lapointe, J. & Yokoyama, S. (1996) J. Mol. Biol. 256, 685-700]. In the present study, we attempted to switch the identity of tRNAAsp, which has a sequence similar to that of tRNAGlu, and consequently possesses many nucleotide residues corresponding to the Glu identity determinants (U35, C36, A37, G1*C72, and U11*A24). A simple transplantation of the rest of the major determinants (U34, U2*A71, U13*G22**Alpha46, and Delta47) to the framework of tRNAAsp did not result in a sufficient switch of the tRNAAsp identity to Glu. To confer an optimal glutamate accepting activity to tRNAAsp, two other elements, C4*G69 in the middle of the acceptor stem and C12*G23**C9 in the augmented D helix, were required. Consistently, the two base pairs, C4*G69 and C12*G23, in tRNAGlu had been shown to exist in the interface with glutamyl-tRNA synthetase (GluRS) by phosphate-group footprinting. We also found the two elements in the framework of tRNAGln, and determined that their contributions successfully changed the identity of tRNAGln to Glu in the previous study. By the identity-determinant set (C4*G69 and C12*G23**C9 in addition to U34, U35, C36, A37, G1*C72, U2*A71, U11*A24, U13*G22**Alpha46, and Delta47) the activity of GluRS was optimized and efficient discrimination from the noncognate tRNAs was achieved.  (+info)

tRNA synthetase mutants of Escherichia coli K-12 are resistant to the gyrase inhibitor novobiocin. (7/1309)

In previous studies we demonstrated that mutations in the genes cysB, cysE, and cls (nov) affect resistance of Escherichia coli to novobiocin (J. Rakonjac, M. Milic, and D. J. Savic, Mol. Gen. Genet. 228:307-311, 1991; R. Ivanisevic, M. Milic, D. Ajdic, J. Rakonjac, and D. J. Savic, J. Bacteriol. 177:1766-1771, 1995). In this work we expand this list with mutations in rpoN (the gene for RNA polymerase subunit sigma54) and the tRNA synthetase genes alaS, argS, ileS, and leuS. Similarly to resistance to the penicillin antibiotic mecillinam, resistance to novobiocin of tRNA synthetase mutants appears to depend upon the RelA-mediated stringent response. However, at this point the overlapping pathways of mecillinam and novobiocin resistance diverge. Under conditions of stringent response induction, either by the presence of tRNA synthetase mutations or by constitutive production of RelA protein, inactivation of the cls gene diminishes resistance to novobiocin but not to mecillinam.  (+info)

Progress toward the evolution of an organism with an expanded genetic code. (8/1309)

Several significant steps have been completed toward a general method for the site-specific incorporation of unnatural amino acids into proteins in vivo. An "orthogonal" suppressor tRNA was derived from Saccharomyces cerevisiae tRNA2Gln. This yeast orthogonal tRNA is not a substrate in vitro or in vivo for any Escherichia coli aminoacyl-tRNA synthetase, including E. coli glutaminyl-tRNA synthetase (GlnRS), yet functions with the E. coli translational machinery. Importantly, S. cerevisiae GlnRS aminoacylates the yeast orthogonal tRNA in vitro and in E. coli, but does not charge E. coli tRNAGln. This yeast-derived suppressor tRNA together with yeast GlnRS thus represents a completely orthogonal tRNA/synthetase pair in E. coli suitable for the delivery of unnatural amino acids into proteins in vivo. A general method was developed to select for mutant aminoacyl-tRNA synthetases capable of charging any ribosomally accepted molecule onto an orthogonal suppressor tRNA. Finally, a rapid nonradioactive screen for unnatural amino acid uptake was developed and applied to a collection of 138 amino acids. The majority of glutamine and glutamic acid analogs under examination were found to be uptaken by E. coli. Implications of these results are discussed.  (+info)

*Aminoacyl tRNA synthetase

Amino Acyl-tRNA Synthetases at the US National Library of Medicine Medical Subject Headings (MeSH) AARS human gene location in ... An aminoacyl tRNA synthetase (aaRS) is an enzyme that attaches the appropriate amino acid onto its tRNA. It does so by ... In humans, the 21 different types of aa-tRNA are made by the 21 different aminoacyl-tRNA synthetases, one for each amino acid ... TARS (gene) "tRNA Synthetases". Retrieved 2007-08-18. "Molecule of the Month: Aminoacyl-tRNA Synthetases High Fidelity". ...

*Peter G. Schultz

This is accomplished by screening libraries of mutant amino acyl tRNA synthetases for mutants which charge nonsense-codon tRNAs ... The organism which expresses such a synthetase can then be genetically programmed to incorporate the unnatural amino acid into ... Normally, the unnatural amino acid itself must be synthesized in the lab and supplied to the organism by adding it to the ... The unnatural amino acid must also be able to pass through the organism's cell membrane into the interior of the organism. More ...

*Stephen A. Cusack

These are exemplified by work on amino acyl tRNA synthetases, crucial to protein synthesis in all living organisms and analyses ... Thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)". Science. New York, N.Y. 263 (5152): 1404-10. doi:10.1126/science. ... "A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å". Nature. ...

*Mimiviridae

... transfer RNA and amino-acyl-tRNA synthetases in mimiviruses. Intervirology 56(6):364-375. doi: 10.1159/000354557 Morgan Gaia et ... Virus Res 117(1):145-155 Colson P, Fournous G, Diene SM, Raoult D (2013) Codon usage, amino acid usage, ...

*List of MeSH codes (D08)

... amino acyl-trna synthetases MeSH D08.811.464.263.200.050 --- alanine-tRNA ligase MeSH D08.811.464.263.200.100 --- arginine-tRNA ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 --- leucine-trna ligase MeSH D08.811.464.263.200.550 --- lysine-trna ligase ... glutamate-trna ligase MeSH D08.811.464.263.200.350 --- glycine-trna ligase MeSH D08.811.464.263.200.400 --- histidine-trna ... phenylalanine-trna ligase MeSH D08.811.464.263.200.750 --- serine-trna ligase MeSH D08.811.464.263.200.800 --- threonine-tRNA ...

*Adenosine triphosphate

Aminoacyl-tRNA synthetase enzymes consume ATP in the attachment tRNA to amino acids, forming aminoacyl-tRNA complexes. ... Dozens of ATP equivalents are generated by the beta-oxidation of a single long acyl chain. The acetyl-CoA produced by beta- ... Aminoacyl transferase binds AMP-amino acid to tRNA. The coupling reaction proceeds in two steps: aa + ATP --> aa-AMP + PPi aa- ... AMP + tRNA --> aa-tRNA + AMP The amino acid is coupled to the penultimate nucleotide at the 3′-end of the tRNA (the A in the ...

*Metabolism

This aminoacyl-tRNA precursor is produced in an ATP-dependent reaction carried out by an aminoacyl tRNA synthetase. This ... The acyl chains in the fatty acids are extended by a cycle of reactions that add the acyl group, reduce it to an alcohol, ... lack all amino acid synthesis and take their amino acids directly from their hosts. All amino acids are synthesized from ... 855-6. ISBN 0-7216-0240-1. Ibba M, Söll D (2001). "The renaissance of aminoacyl-tRNA synthesis". EMBO Rep. 2 (5): 382-7. doi: ...

*Translation (biology)

Aminoacyl-tRNA synthetases that mispair tRNAs with the wrong amino acids can produce mischarged aminoacyl-tRNAs, which can ... The correct amino acid is covalently bonded to the correct transfer RNA (tRNA) by amino acyl transferases. The amino acid is ... Aminoacyl tRNA synthetases (enzymes) catalyze the bonding between specific tRNAs and the amino acids that their anticodon ... The tRNA in the E site leaves and another aminoacyl-tRNA enters the A site to repeat the process. After the new amino acid is ...

*SARS (gene)

SARS belongs to the class II amino-acyl tRNA family and is found in all humans; its encoded enzyme, seryl-tRNA synthetase, is ... function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic ... function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic ... Heckl M, Busch K, Gross HJ (May 1998). "Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA synthetase: ...

*Biosynthesis

This reaction, called tRNA charging, is catalyzed by aminoacyl tRNA synthetase. A specific tRNA synthetase is responsible for ... Succinyl-diaminopimelate desuccinylase catalyzes the removal of acyl group from N-succinyl-L,L-diaminopimelic acid to yield L,L ... Aminoacyl − AMP + tRNA ↽ − − ⇀ aminoacyltRNA + AMP {\displaystyle {\ce {{Aminoacyl-AMP}+ tRNA <=> {aminoacyl-tRNA}+ AMP}}} ... both of which are catalyzed by aminoacyl tRNA synthetase, produces a charged tRNA that is ready to add amino acids to the ...

*Valine-tRNA ligase

VARS Berg P, Bergmann FH, Ofengand EJ, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid ... Other names in common use include valyl-tRNA synthetase, valyl-transfer ribonucleate synthetase, valyl-transfer RNA synthetase ... Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The ... This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis. As of late 2007, 5 ...

*Methionine-tRNA ligase

Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The ... effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA ... Other names in common use include methionyl-tRNA synthetase, methionyl-transfer ribonucleic acid synthetase, methionyl-transfer ... This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid metabolism, and aminoacyl-trna ...

*Isoleucine-tRNA ligase

Berg P, Bergmann FH, Ofengand EJ, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. ... isoleucyl-transfer RNA synthetase, isoleucine-transfer RNA ligase, isoleucine-tRNA synthetase, and isoleucine translase. This ... Other names in common use include isoleucyl-tRNA synthetase, isoleucyl-transfer ribonucleate synthetase, ... Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The ...

*Leucine-tRNA ligase

Leucyl-tRNA synthetase ALLEN EH, GLASSMAN E, SCHWEET RS (1960). "Incorporation of amino acids into ribonucleic acid. I. The ... Berg P, Bergmann FH, Ofengand EJ & Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. ... leucyl-transfer RNA synthetase, leucyl-transfer ribonucleic acid synthetase, leucine-tRNA synthetase, and leucine translase. ... Other names in common use include leucyl-tRNA synthetase, leucyl-transfer ribonucleate synthetase, ...

*Mitochondrial matrix

β-Oxidation uses pyruvate carboxylase, Acyl-CoA dehydrogenase, and 𝛽-Ketothiolase. Amino acid production is facilitated by ... Succinyl-CoA Synthetase, Fumarase, and Malate dehydrogenase. The Urea Cycle is facilitated by Carbamoyl phosphate synthetase I ... Protein synthesis makes use of mitochondrial DNA, RNA, and tRNA. Regulation of processes makes use of ions(Ca2+/K+/Mg+). ... These amino acids are then used either within the matrix or transported into the cytosol to produce proteins. Regulation within ...

*Mupirocin

A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase". J. Biol. Chem. 269 (39): 24304-9. ... In E. coli IleRS, a single amino acid mutation was shown to alter mupirocin resistance. MuH is linked to the acquisition of a ... The mupirocin pathway also contains several tandem acyl carrier protein doublets or triplets. This may be an adaptation to ... Yanagisawa T, Lee JT, Wu HC, Kawakami M (September 1994). "Relationship of protein structure of isoleucyl-tRNA synthetase with ...

*Transfer-messenger RNA

Most conserved is the primary sequence of the amino acyl acceptor stem. This portion of the molecule has an invariable A ... Following the addition of CCA at the 3' discriminator nucleotide, the tmRNA can be charged by alanyl-tRNA synthetase with ... including the acceptor stem with elements like those in alanine tRNA that promote its aminoacylation by alanine-tRNA ligase. It ... P2 is a helix of variable length (3 to 10 base pairs) and corresponds to the anticodon stem of tRNAs, yet without an anticodon ...

*Stringent response

relC) and the ribosome-associated (p)ppGpp synthetase I, RelA; deacylated tRNA bound in the ribosomal A-site is the primary ... This in turn causes the cell to divert resources away from growth and division and toward amino acid synthesis in order to ... A Battesti; E Bouveret (2006). "Acyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to ... "Thermodynamic characterization of ppGpp binding to EF-G or IF2 and of initiator tRNA binding to free IF2 in the presence of GDP ...

*Chromosome 12 (human)

ACAD10: encoding protein Acyl-CoA dehydrogenase family, member 10 ACSS3: encoding protein Acyl-CoA synthetase short-chain ... encoding enzyme tRNA pseudouridine synthase A PUS7L: encoding enzyme Pseudouridylate synthase 7 homolog-like protein RAB3IP: ... encoding protein a protein of 377 amino acid residues FAM60A: encoding protein FAM60A FAM186B: encoding protein Protein FAM186B ... "genetype trna"[Properties] OR "genetype scrna"[Properties] OR "genetype snrna"[Properties] OR "genetype snorna"[Properties]) ...

*MOP flippase

It is encoded by the pAgK84 plasmid of A. tumefaciens and targets a tRNA synthetase. The agnG gene encodes a protein of 496 aas ... The protein members of the PST family are generally of 400-500 amino acyl residues in length and traverse the membrane as ... The bacterial proteins are of about 450 amino acyl residues in length and exhibit 12 putative transmembrane segments (TMSs). ... "Major biocontrol of plant tumors targets tRNA synthetase". Science. 309 (5740): 1533. doi:10.1126/science.1116841. ISSN 1095- ...

*List of EC numbers (EC 6)

EC 6.1.1.1: tyrosine-tRNA ligase EC 6.1.1.2: tryptophan-tRNA ligase EC 6.1.1.3: threonine-tRNA ligase EC 6.1.1.4: leucine-tRNA ... acyl-carrier-protein) ligase EC 6.2.1.21: Covered by EC 6.2.1.30 EC 6.2.1.22: (citrate (pro-3S)-lyase) ligase EC 6.2.1.23: ... 5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase EC 6.3.2.27: The activity is covered by two independent enzymes, EC ... indoleacetate-lysine synthetase EC 6.3.2.21: ubiquitin-calmodulin ligase EC 6.3.2.22: Now EC 6.3.1.14 EC 6.3.2.23: ...

*Enzyme kinetics

Ward WH, Fersht AR (July 1988). "Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of- ... In these serine proteases, the E* intermediate is an acyl-enzyme species formed by the attack of an active site serine residue ... by site-directed mutagenesis of conserved amino acid residues, or by studying the behaviour of the enzyme in the presence of ... Allosteric enzymes include mammalian tyrosyl tRNA-synthetase, which shows negative cooperativity, and bacterial aspartate ...

*Clonal hypereosinophilia

The ACSL6 gene encodes a protein, CSL6 acyl-CoA synthetase long-chain family member 6 (or ACSL6 protein). This protein is a ... "DTD1 D-tyrosyl-tRNA deacylase 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2017-04-17. Gotlib J ( ... Rare patients with hypereosinophilia carry a somatic point mutation in the JAK2 gene which encodes for the amino acid ... by charging fatty acids with Coenzyme A to form acyl-CoA. This function can not only alter fatty acid metabolism but also ...

*Transferase

Further, this category also differentiates between amino-acyl and non-amino-acyl groups. Peptidyl transferase is a ribozyme ... it catalyzes the transfer of a peptide to an aminoacyl-tRNA, following this reaction: peptidyl-tRNAA + aminoacyl-tRNAB ⇌ {\ ... Fitzgerald DK, Brodbeck U, Kiyosawa I, Mawal R, Colvin B, Ebner KE (Apr 1970). "Alpha-lactalbumin and the lactose synthetase ... The transfer involves the removal of the growing amino acid chain from the tRNA molecule in the A-site of the ribosome and its ...

*Housekeeping gene

002047 glycyl-tRNA synthetase HARS NM_002109 histidyl-tRNA synthetase HARS2 NM_012208 histidyl-tRNA synthetase 2, mitochondrial ... macrophage migration inhibitory factor TAPBP ADRBK1 can downregulate response to epinephrine AGPAT1 acyl 3 phosphoglycerol acyl ... ARHGEF2 Rho guanine nucleotide exchange factor ARMET Mesencephalic astrocyte-derived neurotrophic factor AES amino terminal ... 005051 glutaminyl-tRNA synthetase RARS NM_002884 arginyl-tRNA synthetase RARS2 NM_020320 arginyl-tRNA synthetase 2, ...
The aminoacyl-tRNA synthetases (EC 6.1.1.) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices, and are mostly dimeric or multimeric, containing at least three conserved regions. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2-hydroxyl of the tRNA, while, in class II reactions, the 3-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, ...
The tRNA content and aminoacyl-tRNA synthetases of regenerating liver in the phase of rapid growth were compared with those of livers from both intact and sham-operated rats. At 48 h after hepatectomy, the amount of active tRNA (called total acceptor capacity) is significantly higher in regenerating liver than in control livers, owing to a general, possibly not uniform, increase in the various tRNA families, which suggests that it may contribute to the increased protein synthesis and to decreased protein degradation as well. The activities of most, but not of all, aminoacyl-tRNA synthetases in cell sap of regenerating liver tend to be greater than normal. Increased activity of histidyl-tRNA synthetase fits in with the possibility that the mechanisms that control the rate of protein degradation through aminoacylation of tRNAHis in cultured cells [Scornik (1983) J. Biol. Chem. 258, 882-886] also operate in the liver and play a role in regeneration. Sedimentation analysis of cell sap in sucrose ...
Aminoacyl‐tRNA synthetases (aaRSs) comprise an ancient, diverse enzyme family that catalyzes specific attachment of amino acids to their cognate tRNAs and ensures the accurate translation of the genetic code in the first step of protein synthesis (Carter, 1993; Martinis and Schimmel, 1996). The aminoacylation reaction is accomplished by a two‐step process: (a) activation of amino acids with ATP, forming aminoacyl adenylate, and (b) transfer of the aminoacyl residue to the 3′‐end of tRNA (Ibba and Söll, 2000). In this two‐step reaction, each tRNA synthetase molecule must select and activate its cognate amino acid from the cellular pool of 20 different proteinaceous amino acids. Because of the structural similarity of some amino acids, aaRSs really have difficulties in accurately discriminating cognate substrate from others (Baldwin and Berg, 1966; Loftfield and Vanderjagt, 1972). High fidelity in the amino‐acid selection process, which in some cases depends on hydrolytic editing to ...
Aminoacyl-tRNA synthetases are a group of enzymes which activate amino acids and transfer them to specific tRNA molecules as the first step in protein biosynthesis. In prokaryotic organisms there are at least twenty different types of aminoacyl-tRNA synthetases, one for each different amino acid. In eukaryotes there are generally two aminoacyl-tRNA synthetases for each different amino acid: one cytosolic form and a mitochondrial form ...
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2012 ...
wrt-10 encodes a hedgehog-like protein, with an N-terminal signal sequence, a Wart domain, and a C-terminal region of low-complexity sequence. WRT-10 is expressed in both male and hermaphrodite intestine. the Wart domain is predicted to form a cysteine-crosslinked protein involved in intercellular signalling, and it has subtle similarity to the N-terminal Hedge domain of HEDGEHOG proteins. WRT-10 is required for normal growth to full size and locomotion. both of these requirements may reflect common defects in cholesterol-dependent hedgehog-like signalling or in vesicle trafficking. [Source: WormBase]wrt-10 encodes a hedgehog-like protein, with an N-terminal signal sequence, a Wart domain, and a C-terminal region of low-complexity sequence. WRT-10 is expressed in both male and hermaphrodite intestine. the Wart domain is predicted to form a cysteine-crosslinked protein involved in intercellular signalling, and it has subtle similarity to the N-terminal Hedge domain of HEDGEHOG proteins. WRT-10 is ...
Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases. J. Biol. Chem. 261 (23), 10610-10617 (1986 ...
Aminoacyl-tRNA synthetases (EC 6.1.1.-) [1] are a group of enzymes which activate amino acids and transfer them to specific tRNA molecules as the first step in protein biosynthesis. In prokaryotic organisms there are at least twenty different types of aminoacyl-tRNA synthetases, one for each different amino acid. In eukaryotes there are generally two aminoacyl-tRNA synthetases for each different amino acid: one cytosolic form and a mitochondrial form. While all these enzymes have a common function, they are widely diverse in terms of subunit size and of quaternary structure. A few years ago it was found [2] that several aminoacyl-tRNA synthetases share a region of similarity in their N-terminal section, in particular the consensus tetrapeptide His-Ile-Gly-His (HIGH) is very well conserved. The HIGH region has been shown [3] to be part of the adenylate binding site. The HIGH signature has been found in the aminoacyl-tRNA synthetases specific for arginine, cysteine, glutamic acid, glutamine, ...
My group uses X-ray crystallography as a central technique to study the structure-function relationships of complexes involving RNA of various kinds in eukaryotic cells. This includes the transcription/replication machinery of segmented negative strand RNA viruses (e.g. influenza), complexes involved in sorting of Pol II transcripts into their appropriate processing pathways and innate immune system pattern recognition receptors, notably the response to viral RNA via Rig-I like helicases.. Keywords: Protein-RNA recognition / aminoacyl tRNA synthetases / RNA metabolism / virus structure / influenza virus polymerase / innate immunity / Rig-I like helicases / X-ray crystallography. Subject area(s): Microbiology, Virology & Pathogens , RNA , Structural Biology & Biophysics. ...
As mentioned above, not all archaea possess a class I-type LysRS. For example, the crenarchaeotes Pyrobaculum aerophilum (S. Fitz-Gibbon, unpublished data) and Sulfolobus solfataricus (Sensenet al. 1996; C. W. Sensen, personal communication) both contain only class II-type LysRS proteins. Closer examination of these crenarchaeal sequences shows that they are more similar to each other than to any other LysRS and that they have reasonably high homology to bacterial proteins (e.g., both show over 43% identity at the amino acid level to Thermotoga maritima LysRS). This last observation in particular suggests that these crenarchaeal class II LysRS might have been acquired from bacteria.. The apparent two-way transfer of the different LysRS encoding genes, both to and from the archaeal kingdom, has provided clear evidence of the dynamic nature of aminoacyl-tRNA synthetase evolution. This is in stark contrast to previous predictions that suggested that the obvious link between the genetic code and the ...
Accepted name: serine tRNA ligase. Reaction: ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer. Other name(s): seryl-tRNA synthetase; SerRS; seryl-transfer ribonucleate synthetase; seryl-transfer RNA synthetase; seryl-transfer ribonucleic acid synthetase; serine translase. Systematic name: L-serine:tRNASer ligase (AMP-forming). Comments: This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-48-7. References:. 1. Katze, J.R. and Konigsberg, W. Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli. J. Biol. Chem. 245 (1970) 923-930. [PMID: 4906848]. 2. Makman, M.H. and Cantoni, G.L. Isolation of seryl and phenylalanyl ribonucleic acid synthetases from bakers yeast. Biochemistry 4 (1965) 1434-1442.. 3. Webster, L.T. and ...
Figure 1: A parallel genetic code. There are several major challenges in genetically encoding multiple unnatural amino acids into proteins in living cells. First, unique new codons are required that can be used to encode the incorporation of unnatural amino acids at specific sites in proteins. Since the 64 triplet codons are used in the genome of most organisms for encoding natural proteins additional codons (such as quadruplet codons) might be used to encode the incorporation of unnatural amino acids. Second, new aminoacyl-tRNA synthetase tRNA pairs that are orthogonal to the aminoacyl-tRNA synthetase/tRNA pairs in the host organism, and that uniquely direct the incorporation of an unnatural amino acid in response to a unique codon, are required. Finally the scope of cellular protein translation is limited to alpha-L amino acids and their close analogs, and alteration of the ribosome and potentially other components of the translational machinery are required to increase the chemical scope of ...
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. They are a family of twenty enzymes, one for each amino acid. By coupling an amino acid to a specific RNA triplet, the anticodon, they are responsible for interpretation of the genetic code. In addition to this translational, canonical role, several aminoacyl-tRNA synthetases also fulfill nontranslational, moonlighting functions. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes ...
Background Aminoacyl-tRNA synthetases (AARSs) catalyze the first step of protein synthesis. We also established a strategy to check the natural activity of rhTyrRS by calculating aminoacylation and IL-8 launch in rhTyrRS-treated HL-60 cells. Conclusions The characterization of purified rhTyrRS indicated that proteins could be found in pharmacokinetic and pharmacodynamic research. and animal research could possibly be carried out to judge its toxic and pharmacologic results then. In this scholarly study, rhTyrRS was indicated at a higher level in and purified for potential preclinical testing. Strategies Cells and antibodies The skilled stress BL21 (F-ompT hsdS (rB-mB-) gal dcm; providded by aTyr Pharma) was utilized as the sponsor for rhTyrRS manifestation. This stress was transformed using the pET24a inducible manifestation vector where the His-tag series was deleted as well as the T7 promoter was changed having a Tac promoter. A mouse anti-human IL-8 monoclonal antibody ...
QARS, DARS, KARS. The current publication by Zhang and collaborators give us an interesting refresher course on basic molecular biology, particularly a section of the cellular machinery that I didnt believe to be relevant to human genetic epilepsies - tRNAs. In humans the amino acids are attached to the tRNAs through 37 different forms of tRNA synthetases, 17 of them only present in mitochondria. The names of the tRNA synthetases is derived from the specific amino acid symbol, followed by the suffix -ARS. Amongst the various tRNA synthetases implicated in human disease, two disease-related aaRS occur in a functional complex with QARS, the multisynthetase complex. These two aaRS are KARS and DARS. The KARS gene coding for the lysine tRNA synthetase has been found to be mutated in a particular form of Charcot-Marie-Tooth disease and, separately from this, nonsyndromic hearing loss. Mutations in the DARS gene coding for the asparate tRNA synthetase cause an inherited white matter disorder with leg ...
aminoacyl tRNA synthetase p18 component: shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1; amino acid sequence given in first source
... - reflects the multidimensional character of chemical biology, focusing in particular on the fundamental science of biological structures and systems, the use of chemical and biological techniques to elucidate
Eprs - mouse gene knockout kit via CRISPR, 1 kit. |dl||dt|Kit Component:|/dt||dd|- |strong|KN305300G1|/strong|, Eprs gRNA vector 1 in |a href=http://www.origene.com/CRISPR-CAS9/Detail.
Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with…
Semantic Scholar extracted view of [14C]erythromycin-ribosome complex formation and non-enzymatic binding of aminoacyl-transfer RNA to ribosome-messenger RNA complex. by Kohichi Tanaka et al.
Rabbit polyclonal Glutamyl Prolyl tRNA synthetase antibody validated for WB, IHC and tested in Human. With 4 independent reviews. Immunogen corresponding to…
Mouse monoclonal valyl tRNA synthetase antibody [VARSA7E6] validated for WB, Dot and tested in Human. Immunogen corresponding to recombinant fragment
Looking for online definition of aminoacyl-tRNA synthetases in the Medical Dictionary? aminoacyl-tRNA synthetases explanation free. What is aminoacyl-tRNA synthetases? Meaning of aminoacyl-tRNA synthetases medical term. What does aminoacyl-tRNA synthetases mean?
Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene. Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. HARS has been shown to interact with EEF1B2 and EEF1G. GRCh38: Ensembl release 89: ENSG00000170445 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000001380 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". "Entrez Gene: HARS ...
Aminoacyl tRNA synthetases play a central role in protein synthesis by charging tRNAs with amino acids. Yeast mitochondrial lysyl tRNA synthetase (Msk1), in addition to the aminoacylation of mitochondrial tRNA, also functions as a chaperone to facilitate the import of cytosolic lysyl tRNA. In this report, we show that human mitochondrial Kars (lysyl tRNA synthetase) can complement the growth defect associated with the loss of yeast Msk1 and can additionally facilitate the in vitro import of tRNA into mitochondria. Surprisingly, the import of lysyl tRNA can occur independent of Msk1 in vivo. This suggests that an alternative mechanism is present for the import of lysyl tRNA in yeast.
1QRT: Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP.
The SRP9/14 heterodimer is the latest member of a growing family of small α/β RNA binding proteins examples of which are: the ribonucleoprotein (RNP) domain (Nagai et al., 1990; Oubridge et al., 1994); the double‐stranded RNA binding domain (dsRBD) (Farrandon et al., 1994; Bycroft et al., 1995; Kharrat et al., 1995); the K homology (KH) domain (Musco et al., 1996); the coat protein of bacteriophage MS2 (Valegård et al., 1990); the translational initiation factor IF3 (Biou et al., 1995); the S1 RNA binding domain (Bycroft et al., 1997); and many ribosomal proteins (Nagai, 1996). The RNP and KH domains, as well as several ribosomal proteins (Liljas and Garber, 1995), belong to the so‐called split α‐β‐α motif differing from the dsRBD, MS2 and SRP9/14 where the sheet is a β‐meander. In aminoacyl‐tRNA synthetases, a number of different tRNA anti‐codon binding modules have also been characterized (Cusack, 1995; Moras and Poterszman, 1996). Interestingly, RNA and DNA binding ...
In enzymology , a valine-tRNA ligase ( EC 6.1.1.9 ) is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are ATP , L-valine , and tRNA(Val) , whereas its 3 products are AMP , diphosphate , and L-valyl-tRNA(Val) . This enzyme belongs to the family of ligases , to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-valine:tRNAVal ligase (AMP-forming) . Other names in common use include valyl-tRNA synthetase , valyl-transfer ribonucleate synthetase , valyl-transfer RNA synthetase , valyl-transfer ribonucleic acid synthetase , valine transfer ribonucleate ligase , and valine translase . This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis . Structural studies As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GAX , 1IVS , 1IYW , 1WK9 , and 1WKA . See also VARS References Berg P, Bergmann FH, Ofengand
In contrast with most aminoacyl-tRNA synthetases, the lysyl-tRNA synthetase of Escherichia coli is coded for by two genes, the normal lysS gene and the inducible lysU gene. During its purification from E. coli K12, lysyl-tRNA synthetase was monitored by its aminoacylation and adenosine(5′)tetraphospho(5′)adenosine (Ap4A) synthesis activities. Ap4A synthesis was measured by a new assay using DEAE-cellulose filters. The heterogeneity of lysyl-tRNA synthetase (LysRS) was revealed on hydroxyapatite; we focused on the first peak, LysRS1, because of its higher Ap4A/lysyl-tRNA activity ratio at that stage. Additional differences between LysRS1 and LysRS2 (major peak on hydroxyapatite) were collected. LysRS1 was eluted from phosphocellulose in the presence of the substrates, whereas LysRS2 was not. Phosphocellulose chromatography was used to show the increase of LysRS1 in cells submitted to heat shock. Also, the Mg2+ optimum in the Ap4A-synthesis reaction is much higher for LysRS1. LysRS1 showed a ...
Although the nucleotides in tRNA required for aminoacylation are conserved in evolution, bacterial aminoacyl-transfer RNA synthetases are unable to acylate eukaryotic tRNA. The cross-species barrier may be due to the absence of eukaryote-specific domains from bacterial aminoacyl-transfer RNA synthetases. Here we show that whereas Escherichia coli CysRS cannot acylate human tRNA(Cys), the fusion of a eukaryote-specific domain of human CysRS overcomes the cross-species barrier in human tRNA(Cys). In addition to enabling recognition of the sequence differences in the tertiary core of tRNA(Cys), the fused eukaryotic domain redirects the specificity of E. coli CysRS from the A37 present in bacterial tRNA(Cys) to the G37 in mammals. Further experiments show that the accuracy of codon recognition on the ribosome was also highly sensitive to the A37G transition in tRNA(Cys). These results raise the possibility of the development of tRNA nucleotide determinants for aminoacylation being interdependent with those
This invention provides methods and compositions for incorporation of an unnatural amino acid into a peptide using an orthogonal aminoacyl tRNA synthetase/tRNA pair. In particular, an orthogonal pair
Background: Electronic Patient Records (EPRs) are being introduced into many healthcare organisations around the world. In the UK, EPRs are seen as one mechanism through which the NHS can become safer and more efficient. The policy and financial support for NHS hospitals to implement these systems, implies a strong evidence base supporting the rationale that electronic records improve health outcomes and quality of care. In reality, there is limited evidence to support this, with a lack of understanding as to the best approaches to and the benefits, barriers and impact of implementing EPRs; particularly within the NHS. In this thesis, the implementation of EPRs into NHS secondary care organisations is explored. Methods: A range of methods were used to explore the implementation of EPRs into NHS secondary care organisations. A policy analysis studied national NHS IT policy documents and evaluations of national NHS IT policy between 1998 and 2015 to investigate whether progress has been made in ...
The rapid progress of research in the tRNA field and recent advances in the understanding of the molecular basis of specificity in tRNA: protein interactions make it necessary to have all of the accumulated information in an easily accessible form. The purpose of this book is to fulfill that need by providing an up-to-date account of all aspects of research on transfer RNA, including its structure, biosynthesis, and interactions with the many proteins involved in protein biosynthesis. Beginning with an historical account, the book covers a broad area of research on tRNA biosynthesis, the different functions of tRNA in the genetic decoding process, its association with many different proteins, and the emerging rules governing the specificity of their interactions. In view of the impressive progress made in the last few years, several of the chapters are devoted to discussion of aminoacyl-tRNA synthetase tRNA interactions. An appendix containing the structural formulae of all modified nucleosides found in
Aminoacyl-tRNA synthetases (aaRSs) are modular enzymes globally conserved in the three kingdoms of life. All catalyze the same two-step reaction, i.e., the attachment of a proteinogenic amino acid on their cognate tRNAs, thereby mediating the correct expression of the genetic code. In addition, some aaRSs acquired other functions beyond this key role in translation. Genomics and X-ray crystallography have revealed great structural diversity in aaRSs (e.g., in oligomery and modularity, in ranking into two distinct groups each subdivided in 3 subgroups, by additional domains appended on the catalytic modules). AaRSs show huge structural plasticity related to function and limited idiosyncrasies that are kingdom or even species specific (e.g., the presence in many Bacteria of non discriminating aaRSs compensating for the absence of one or two specific aaRSs, notably AsnRS and/or GlnRS). Diversity, as well, occurs in the mechanisms of aaRS gene regulation that are not conserved in evolution, notably ...
Complete information for CARS2 gene (Protein Coding), Cysteinyl-TRNA Synthetase 2, Mitochondrial, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for EPRS gene (Protein Coding), Glutamyl-Prolyl-TRNA Synthetase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
JUPITER, FL - For the past several years, Min Guo, an assistant professor at The Scripps Research Institute (TSRI), has focused on the intricate actions of an ancient family of catalytic enzymes that play a key role in translation, the process of producing proteins. These complex enzymes are a group of fundamental molecules that make building blocks for protein production. Present in every cell, these enzymes-known as aminoacyl-transfer RNA synthetases (tRNA synthetases)-select the proper amino acids and assign them to transfer RNAs to make a protein in the ribosome. As an essential step of determining the genetic code, tRNA synthetases have been around for billions of years. However, this essential part of the protein-making machine did not stop evolving. Now, in a new study published online ahead of print on November 15, 2012, by the journal Molecular Cell, Guo, Ehud Razin of The Institute for Medical Research Israel-Canada, and a large team of international scientists have shown that this ...
Tryptophanyl tRNA synthetase兔单克隆抗体[EPR3423](ab109213)可与小鼠, 大鼠, 人样本反应并经WB, IHC, Flow Cyt实验严格验证。所有产品均提供质保服务,中国75%以上现货。
Mouse Monoclonal Anti-Tryptophanyl tRNA synthetase Antibody (3A12) [PE]. Validated: WB, ELISA, ICC/IF, IP. Tested Reactivity: Human. 100% Guaranteed.
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Adenosine monophosphate (AMP) is a key cellular metabolite regulating energy homeostasis and signal transduction. AMP is also a product of various enzymatic reactions, many of which are dysregulated during disease conditions. Thus, monitoring the activities of these enzymes is a primary goal for developing modulators for these enzymes. In this study, we demonstrate the versatility of an enzyme-coupled assay that quantifies the amount of AMP produced by any enzymatic reaction regardless of its substrates. We successfully implemented it to enzyme reactions that use adenosine triphosphate (ATP) as a substrate (aminoacyl tRNA synthetase and DNA ligase) by an elaborate strategy of removing residual ATP and converting AMP produced into ATP; so it can be detected using luciferase/luciferin and generating light ...
Article{pmid25409537, Author=Thibodeaux, C. J. and Ha, T. and van der Donk, W. A. , Title={{A} price to pay for relaxed substrate specificity: a comparative kinetic analysis of the class {I}{I} lanthipeptide synthetases {P}roc{M} and {H}al{M}2}, Journal=J. Am. Chem. Soc., Year=2014, Volume=136, Number=50, Pages=17513--17529, Month=Dec ...
K.NAKANISHI,Y.OGISO,T.NAKAMA,S.FUKAI,O.NUREKI. CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS METHIONYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(MET) AND METHIONYL-ADENYLATE ANOLOGUE. TO BE PUBLISHED ...
July 15 2017 Issue The semi-monthly AARS online Hot Topics Newsletter is an exclusive AARS member benefit! You dont need to spend countless hours perusing your typical online sources when you have this! Stay informed today by becoming an AARS member and receiving the Hot Topics!
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Aminoacyl-tRNA synthetases should ensure high accuracy in tRNA aminoacylation. However, the absence of significant structural differences between amino acids always poses a direct challenge for some aminoacyl-tRNA synthetases, such as leucyl-tRNA synthetase (LeuRS), which require editing function to remove mis-activated amino acids. In the cytoplasm of the human pathogen Candida albicans, the CUG codon is translated as both Ser and Leu by a uniquely evolved CatRNASer(CAG). Its cytoplasmic LeuRS (CaLeuRS) is a crucial component for CUG codon ambiguity and harbors only one CUG codon at position 919. Comparison of the activity of CaLeuRS-Ser919 and CaLeuRS-Leu919 revealed yeast LeuRSs have a relaxed tRNA recognition capacity. We also studied the mis-activation and editing of non-cognate amino acids by CaLeuRS. Interestingly, we found that CaLeuRS is naturally deficient in tRNA-dependent pre-transfer editing for non-cognate norvaline while displaying a weak tRNA-dependent pre-transfer editing ...
Alanine at position 294 (Ala294) within the motif 3 consensus of Escherichia coli phenylalanyl-tRNA synthetase alpha subunit has previously been implicated as a determinant of amino acid specificity. To characterize the role of Ala294, the catalytic effects of amino acid replacements at this position were tested with purified wild-type and mutant phenylalanyl-tRNA synthetases. We show that Ala294 is involved in amino acid binding and that it influences specificity as a determinant of binding pocket size. Replacement of Ala294 by either glycine or serine, thereby increasing or decreasing the size of the binding pocket, respectively, reduces affinity for phenylalanine. The Gly294 mutant shows a relaxed specificity toward synthetic para-halogenated phenylalanine analogues, the apparent dissociation constant Km increasing in direct relation to an increase of the van der Waals radius of the para group, thus confirming the role of position 294 in determining amino acid binding pocket size. For the substrate
For discrimination between threonine and 18 other naturally occurring non-cognate amino acids by the class II aminoacyl-tRNA synthetase specific for threonine, discrimination factors (D) have been determined from Kca and Km values. The lowest values
Translating nucleic acid based information into a protein product is at the heart of the genetic code. Aminoacyl-tRNA synthetases (aaRSs) function is the basis of decoding the genetic code by ligating the cognate tRNA and amino acid together. Given this role, aaRSs maintain an enormous level of specificity for their amino acid and tRNA substrates. This thesis sought to uncover the mechanisms of substrate specificity in aaRSs using glutaminyl- and glutamyl-tRNA synthetases (GlnRS and GluRS, respectively) as model systems. The work addresses the macromolecular coevolution in this subfamily, revealing the nucleic acid recognition signatures within the tRNA utilized by eukaryotic GlnRS and GluRS. Furthermore a rational engineering method discovered that the aforementioned tRNA signatures also assist the corresponding GlxRS in amino acid recognition, a novel concept in genetic code translation. These generalized principles and engineering strategy can be applied to further our understandings in
Although the basic mechanisms of protein synthesis are established and structures of many of the components have been determined, many details remain unknown at the molecular level, particularly the mechanistic details regarding function and regulation of the aminoacyl-tRNA synthetases (AARSs). In addition to being key players in translation, the AARSs are good models for understanding allosteric interactions, in which a binding event triggers enzymatic catalysis at a distant site. Many AARSs bind to the anticodon portion of their matching (cognate) tRNA molecules, and the anticodon-binding site is often tens of Ångstroms removed from the enzyme active site, where amino acid attachment occurs. Efficient anticodon-mediated aminoacylation therefore depends on communication between protein domains. Our lab is investigating the long-range communication in E. coli methionyl-tRNA synthetase (MetRS), an AARS that requires anticodon binding for efficient catalysis yet also aminoacylates a small tRNA ...
The SCOP classification for the Arginyl-tRNA synthetase (ArgRS), N-terminal additional domain superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
Sérine-ARNt ligase La sérine-ARNt ligase, ou séryl-ARNt synthétase, est une ligase qui catalyse les réactions : ATP + L-sérine + ARNtSer ⇌ {\displaystyle \rightleftharpoons } AMP + pyrophosphate + L-séryl-ARNtSer ; ATP + L-sérine + ARNtSec ⇌ {\displaystyle \rightleftharpoons } AMP + pyrophosphate + L-séryl-ARNtSec. Cette enzyme fixe la sérine, un acide α-aminé protéinogène, sur son ARN de transfert, noté ARNtSer. Elle peut également fixer la sérine sur lARN de transfert de la sélénocystéine. Le séryl-ARNtSec nest pas incorporé dans les protéines naissantes par les ribosomes car il nest pas reconnu par les facteurs délongation cellulaires ; en revanche, cest un substrat de la sélénocystéine synthase, qui convertit le séryl-ARNtSec en sélénocystéinyl-ARNtSec à laide de sélénophosphate SePO33-. (en) Katze JR, Konigsberg W, « Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli », J. Biol. Chem., vol. 245, no 5, ...
View Notes - lecture22 from BCH BCH 453 at N.C. State. What is required for translation? mRNA tRNAs tRNA synthetases amino acids ribosomes peptidyl transferase protein
MARS Full-Length MS Protein Standard (NP_004981), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. This gene encodes a member of the class I family of aminoacyl-tRNA synthetases. These enzymes play a critical role in protein biosynthesis by charging tRNAs with their cognate amino acids. The encoded protein is a component of the multi-tRNA synthetase complex and catalyzes the ligation of methionine to tRNA molecules.
11AS: Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase.
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Recognition of tRNAs by alanyl-tRNA synthetases and FemXWv. (A) Sequence of the tRNAAla acceptor stem. The bases essential for formation of UDP-MurNAc-hexapepti
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Uranium atom in PDB 1b3h: Oligo-Peptide Binding Protein Complexed With Lysyl- Cyclohexylalanyl-Lysine
Looking for online definition of Aars in the Medical Dictionary? Aars explanation free. What is Aars? Meaning of Aars medical term. What does Aars mean?
Elongation requires the elongation factors,ref,Stryer, Biochemistry, Seventh edition, 2007: 936,/ref, EF-Tu, EF-Ts and EF-G as well as GTP to supply the energy. Elongation describes the process of aminoacyl tRNA molecules binding to the codon. A [[Peptide bond,peptide bond]] is formed between the amino acid of the tRNA in the P site and the amino acid in the tRNA molecule that has just arrived at the A site; the formation of this peptide bond is catalysed by the 23S subunit. The amino acid in the P site is released from its tRNA molecule and the ribosome moves along so as to transfer the tRNA currently in the A site into the P site. This step is known as transloaction. The uncharged tRNA i.e. tRNA without an amino acid, moves into the E (empty) site. ,ref,http://rpi.edu/dept/bcbp/molbiochem/MBWeb/mb2/part1/translate.htm,/ref,,br ...
About Anand Minajigi. I graduated from the Cell and Molecular Biology graduate program at the University of Vermont. I was engaged in deciphering the mechanism of aminoacylation and editing by aminoacyl-tRNA synthetases during protein synthesis under the guidance of Dr. Chris Francklyn. I joined the Lee group to explore the mechanism of Polycomb targeting in mammals.. Publications ...
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 site on the tRNA molecule that is bound to the aminoacetyl synthetase. In the case of yeast phenylalanine tRNA, this region is located adjacent to the dihydrouridine loop and consists of the four nucleotide pairs bracketed by arrows on the tRNA on page 397. See Chronology, 1971, Dudock et al.; amino acid activation, transfer RNA. ...
refers to tRNA(Arg-Asp) dimeric genes. **, Suppressors, as defined in MIPS annotations, supplemented by items from tables 8 and 10 in Hinnebusch and Liebmann, 1982. Note: Nomenclature of tRNA species generally follows earlier conventions; in some cases, new indices were assigned to those tRNA subspecies that had not unequivocally been numbered thus far or that were detected by sequencing. ...
There is yet no full understanding concerning the issue of how nutrition metabolites are sensed intracellularly. Recent studies have shed some light on the fact that cells through sensing certain metabolite substances such as 1,6 fructose diphosphate, glutamine and arginine, are able to control the significant cellular signal networks, i.e., AMPK and mTORC1. Discovery as such, further stresses the importance of metabolite sensing. However, little is known concerning how cells systematically sense a specific metabolite and their signal transduction. The research team at Fudan which is made up of Professor Zhao Shimin, research associate Xu Wei and Professor Xu Yanhui has been working on this tricky scientific issue for five years, and has recently discovered that not only can tRNA synthetases recognize amino acids and activate tRNAs role in protein synthesis, but they also bear the function of modifying lysine aminoacylation. This breakthrough helps reveal the systematic and functional amino ...
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IARS antibody (isoleucyl-tRNA synthetase) for IHC-P, IP, WB. Anti-IARS pAb (GTX131733) is tested in Human, Rat samples. 100% Ab-Assurance.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid, AA is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs. {ECO:0000269,PubMed:19426743 ...
perosamine synthetase: a dual function enzyme that converts CDP-paratose to CPP-tyvelose; also converts GDP-4-keto-6-deoxymannose to perosamine
Mistranslation can follow two events during protein synthesis: production of non-cognate amino acid:transfer RNA (tRNA) pairs by aminoacyl-tRNA synthetases (aaRSs) and inaccurate selection of aminoacyl-tRNAs by the ribosome. Many aaRSs actively edit non-cognate amino acids, but editing mechanisms are not evolutionarily conserved, and their physiological significance remains unclear. To address the connection between aaRSs and mistranslation, the evolutionary divergence of tyrosine editing by phenylalanyl-tRNA synthetase (PheRS) was used as a model. Certain PheRSs are naturally error prone, most notably a Mycoplasma example that displayed a low level of specificity consistent with elevated mistranslation of the proteome. Mycoplasma PheRS was found to lack canonical editing activity, relying instead on discrimination against the non-cognate amino acid by kinetic proofreading. This mechanism of discrimination is inadequate for organisms where translation is more accurate, as Mycoplasma PheRS failed ...
Expanding the Genetic Code using the PylRS/tRNACUA pair. A. An unnatural amino acid (blue star) is taken up by the cell. It is specifically recognized by an orthogonal aminoacyl-tRNA synthetase and attached to the orthogonal amber suppressor tRNACUA (blue trident), which is decoded on the ribosome in response to an amber codon. Natural amino acids are shown as black ovals. B. Orthogonal synthetase tRNACUA pairs are generated in two steps: import of a heterologous tRNACUA into a host containing a set of natural synthetases (grey) that use natural amino acids, and the subsequent selection of a mutated active site in the orthogonal synthetase to recognize the unnatural amino acid. C. A large library of active site variants of the synthetase is subject to positive selection for activity with either natural or unnatural amino acids, by virtue of their ability to suppress a stop codon in a gene essential for survival. Synthetases using natural amino acids are subsequently removed by a negative ...
In human neutrophils, the synthetic lipopeptide, N-palmitoyl-S-[2,3- bis(palmitoyloxy-(2RS)-propyl]-(R)-cysteinyl-(S)-seryl-(S)-lysyl-( S)-lysyl-(S) -lysyl-(S)-lysine [Pam3CysSer(Lys)4], activates NADPH-oxidase catalyzed superoxide (O2-) formation through pertussis-toxin-sensitive and pertussis-toxin-insensitive mechanisms (Seifert, R., Schultz, G., Richter-Freund, M., Metzger, J., Wiesmüller, K.-H., Jung, G., Bessler, W. G. & Hauschildt, S. (1990) Biochem. J. 267, 795-802). We studied the effects of lipopeptides on differentiation of HL-60 leukemic cells. Pam3CysSer(Lys)4 enhanced phorbol-12-myristate-13-acetate-induced O2- formation (presumably through the expression of components of NADPH oxidase) in a concentration-dependent manner with a half-maximal effect at 100 ng/ml and a maximum at 1 microgram/ml. The effect of the lipopeptide was evident after 24 h and reached a plateau after 48 h. (2S,6S)-2-Palmitoylamino-6,7- bis(palmitoyloxy)heptanoyl-(S)-seryl-(S)-lysyl-(S)-lysyl-(S) ...
Sato, K, "A mammalian cell mutant with an altered alanyl-trna synthetase. Abstr." (1976). Subject Strain Bibliography 1976. 2737 ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Ans. Unambiguous. 9. Once the reading is started at a specific codon, there is no ___________ between codons. Ans. Punctuation. 10. Amino acids are activated by the enzyme_________ in the presence of the coenzyme_________ . Ans. Aminoacyl-tRNA synthetase; ATP. 11. The binding of the mRNA to the 40S ribosomal subunit requires the presence of ___________. Ans. IF-3. 12. The initiation factor is a ___________ factor. Ans. Protein. 13. The complex formed by anticodon of tRNA and IF-I attaches the 60S ribosomal subunits with the release of ___________, ___________, ___________. Ans. IF-1, IF-2, IF-3. 14. The complete ribosome contains two sites ___________ site and ___________ site on the mRNA. Ans. P; A. 15. During the process of initiation, the complete___________ ribosome is formed. Ans. 80S. 16. ________ forms a complex with___________ and the entering aminoacyl-tRNA. Ans. EF-1; GTP. 17. The alpha amino group of the new aminoacyl- tRNA in the A site combines with the carboxyl group of the ...
Harnessing the modular architecture of non-ribosomal peptide synthetases for combinatorial biosynthesis is a longstanding goal in chemical biology. Several recent reports illustrate how computational design and directed evolution can be used to tailor the specificity of these assembly-line enzymes.. ...
Research topics: Functional genomics and biology of tRNA, RNA epigenetics. Translational regulation is related to the dynamic properties of tRNA that constantly change to facilitate stress response and adaptation to new environments and to control gene expression. We developed microarray and high-throughput sequencing methods that measure tRNA abundance, fraction of aminoacylation, misacylation and modification dynamics at the transcriptomic scale. We are exploring roles of tRNA in translational control in mammalian cells.. A central tenet of biology is the accurate flow of information from nucleic acids to proteins through the genetic code. It is commonly believed that translation deviating from the genetic code is avoided at all times. We discovered that mammalian cells can deliberately reprogram the genetic code through tRNA misacylation upon innate immune activation and chemically triggered oxidative stress. We are investigating how regulated mis-translation is used as a mechanism for stress ...
The ribosome uses this mRNA as template and translates each codon by pairing it with appropriate amino acid which is provided by aminoacyl-tRNA (aminoacyl-tRNA contains a complementary anti-codon). The ribosome contains three RNA binding sites as A, P and E. The A site binds an aminoacyl-tRNA; the P site binds a peptidyl-tRNA and E site binds a free tRNA before it exits the ribosome as can be seen in the diagram ...
Structuresof the protein and the unnatural amino acid analogues incorporatedinto the proteins. (A) Native GBP with glucose in the ligand-bindingpocket and Ca2+
October 1 2017 Issue The semi-monthly AARS online Hot Topics Newsletter is an exclusive AARS member benefit! We encourage you to invite your colleagues and patients to get active in the American Acne & Rosacea Society!
A heat-sensitive (hs) leucyl-tRNA synthetase (leuRS) deficient CHO mutant, ts025Cl, was fused with human leukocytes and hybrids isolated in HAT medium at the nonpermissive temperature. Nineteen heat-r
September, 2011 Volume II, Issue II Inside this issue: Guidance for Reporting Reason-able Suspicion 2 Chair Exercises for the Elderly 3 Disease Reporting In Oklahoma 5 Reportable Diseases 6 Keep Your Resi-dents Hydrated 7 EPRS QIS Update 8 9 OSU Workforce Development 9 Training Corner 11 Insider Chat L T C You Should Have Been There!!! Dorya Huser, Chief, Long Term Care If you were among the very fortunate that attended the nursing home provider training this year, you were entertained by a number of very talented and knowledgeable speakers. While I enjoyed them all and may reserve the right to talk about others in future editions of Insider Chat, I want to talk about Kent Radar and try to give you a tiny piece of his message. Mr. Radar is a comedian with what I believe is a serious message but with a very humor-ous and delightful delivery. He focuses on stress relieving strategies and profiles his life and experiences during his presentation. He tells us we are the architects of our own stress ...
September, 2011 Volume II, Issue II Inside this issue: Guidance for Reporting Reason-able Suspicion 2 Chair Exercises for the Elderly 3 Disease Reporting In Oklahoma 5 Reportable Diseases 6 Keep Your Resi-dents Hydrated 7 EPRS QIS Update 8 9 OSU Workforce Development 9 Training Corner 11 Insider Chat L T C You Should Have Been There!!! Dorya Huser, Chief, Long Term Care If you were among the very fortunate that attended the nursing home provider training this year, you were entertained by a number of very talented and knowledgeable speakers. While I enjoyed them all and may reserve the right to talk about others in future editions of Insider Chat, I want to talk about Kent Radar and try to give you a tiny piece of his message. Mr. Radar is a comedian with what I believe is a serious message but with a very humor-ous and delightful delivery. He focuses on stress relieving strategies and profiles his life and experiences during his presentation. He tells us we are the architects of our own stress ...
September, 2011 Volume II, Issue II Inside this issue: Guidance for Reporting Reason-able Suspicion 2 Chair Exercises for the Elderly 3 Disease Reporting In Oklahoma 5 Reportable Diseases 6 Keep Your Resi-dents Hydrated 7 EPRS QIS Update 8 9 OSU Workforce Development 9 Training Corner 11 Insider Chat L T C You Should Have Been There!!! Dorya Huser, Chief, Long Term Care If you were among the very fortunate that attended the nursing home provider training this year, you were entertained by a number of very talented and knowledgeable speakers. While I enjoyed them all and may reserve the right to talk about others in future editions of Insider Chat, I want to talk about Kent Radar and try to give you a tiny piece of his message. Mr. Radar is a comedian with what I believe is a serious message but with a very humor-ous and delightful delivery. He focuses on stress relieving strategies and profiles his life and experiences during his presentation. He tells us we are the architects of our own stress ...
September, 2011 Volume II, Issue II Inside this issue: Guidance for Reporting Reason-able Suspicion 2 Chair Exercises for the Elderly 3 Disease Reporting In Oklahoma 5 Reportable Diseases 6 Keep Your Resi-dents Hydrated 7 EPRS QIS Update 8 9 OSU Workforce Development 9 Training Corner 11 Insider Chat L T C You Should Have Been There!!! Dorya Huser, Chief, Long Term Care If you were among the very fortunate that attended the nursing home provider training this year, you were entertained by a number of very talented and knowledgeable speakers. While I enjoyed them all and may reserve the right to talk about others in future editions of Insider Chat, I want to talk about Kent Radar and try to give you a tiny piece of his message. Mr. Radar is a comedian with what I believe is a serious message but with a very humor-ous and delightful delivery. He focuses on stress relieving strategies and profiles his life and experiences during his presentation. He tells us we are the architects of our own stress ...
September, 2011 Volume II, Issue II Inside this issue: Guidance for Reporting Reason-able Suspicion 2 Chair Exercises for the Elderly 3 Disease Reporting In Oklahoma 5 Reportable Diseases 6 Keep Your Resi-dents Hydrated 7 EPRS QIS Update 8 9 OSU Workforce Development 9 Training Corner 11 Insider Chat L T C You Should Have Been There!!! Dorya Huser, Chief, Long Term Care If you were among the very fortunate that attended the nursing home provider training this year, you were entertained by a number of very talented and knowledgeable speakers. While I enjoyed them all and may reserve the right to talk about others in future editions of Insider Chat, I want to talk about Kent Radar and try to give you a tiny piece of his message. Mr. Radar is a comedian with what I believe is a serious message but with a very humor-ous and delightful delivery. He focuses on stress relieving strategies and profiles his life and experiences during his presentation. He tells us we are the architects of our own stress ...
Genetic information processingProtein synthesistRNA and rRNA base modificationtRNA(Ile)-lysidine synthetase, C-terminal domain (TIGR02433; EC 6.-.-.-; HMM-score: 71.6) ...
The AUA codon-specific isoleucine tRNA (tRNA(Ile)) in eubacteria has the posttranscriptionally modified nucleoside lysidine (L) at the wobble position of the anticodon (position 34). This modification is a lysine-containing cytidine derivative that converts both the codon specificity of tRNA(Ile) from AUG to AUA and its amino acid specificity from methionine to isoleucine. We identified an essential gene (tilS; tRNA(Ile)-lysidine synthetase) that is responsible for lysidine formation in both Bacillus subtilis and Escherichia coli. The recombinant enzyme complexed specifically with tRNA(Ile) and synthesized L by utilizing ATP and lysine as substrates. The lysidine synthesis of this enzyme was shown to directly convert the amino acid specificity of tRNA(Ile) from methionine to isoleucine in vitro. Partial inactivation of tilS in vivo resulted in an AUA codon-dependent translational defect, which supports the notion that TilS is an RNA-modifying enzyme that plays a critical role in the accurate ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
McDowall, K.J., Hernandez, R.G., Lin-Chao, S., and Cohen, S.N. (1993) The ams-1 and rne-3071 temperature-sensitive mutations in the ams gene are in close proximity to each other and cause substitutions within a domain that resembles a product of the Escherichia coli mre locus. J Bacteriol 175: 4245-4249 ...
Streptomyces netropsis two component response regulator-like gene, partial cds; netropsin resistance protein subunit 1 (netP1) and netropsin resistance protein subunit 2 (netP2) genes, complete cds; and acyl-CoA synthetase-like gene, partial ...
ID E4T4I4_PALPW Unreviewed; 339 AA. AC E4T4I4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 08-MAY-2019, entry version 53. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256,HAMAP-Rule:MF_00281}; DE EC=6.1.1.20 {ECO:0000256,HAMAP-Rule:MF_00281}; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256,HAMAP-Rule:MF_00281}; DE Short=PheRS {ECO:0000256,HAMAP-Rule:MF_00281}; GN Name=pheS {ECO:0000256,HAMAP-Rule:MF_00281}; GN OrderedLocusNames=Palpr_1482 {ECO:0000313,EMBL:ADQ79628.1}; OS Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Paludibacteraceae; Paludibacter. OX NCBI_TaxID=694427 {ECO:0000313,EMBL:ADQ79628.1, ECO:0000313,Proteomes:UP000008718}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WB4; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., ...
Sigma-Aldrich offers abstracts and full-text articles by [Muhammed Z Cader, Jingshan Ren, Paul A James, Louise E Bird, Kevin Talbot, David K Stammers].
The genetic incorporation of unnatural amino acids (UAAs) into proteins has been a useful tool for protein engineering. However, most UAAs are expensive, and the method requires a high concentration o
Buy Unnatural Amino Acids (9781617793301): Methods and Protocols: NHBS - Edited By: Loredano Pollegioni and Stefano Servi, Humana Press
Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection / Y H Ahn; S Park; J J Choi; B K Park; K H Rhee; E Kang; S Ahn; Chul Ho Lee; J S Lee; K S Inn; M L Cho; S H Park; K Park; H J Park; J H Lee; J W Park; N H Kwon; H Shim; B W Han; P Kim; J Y Lee; Y Jeon; J W Huh; M Jin; S Kim , 2016 ...
Methods for making glycoproteins, both in vitro and in vivo, are provided. One method involves incorporating an unnatural amino acid into a protein and attaching one or more saccharide moieties to the unnatural amino acid. Another method involves incorporating an unnatural amino acid that includes a saccharide moiety into a protein. Proteins made by both methods can be further modified with additional sugars.
The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This HMM describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this HMM should called methionyl-tRNA synthetase beta chain if and only if the HMM metG hits a separate protein not also hit by this HMM ...
Chinese hamster ovary cell lines that are 1000-fold more resistant to the threonyl-tRNA synthetase inhibitor borrelidin than the sensitive parental cells were isolated after stepwise selection for growth in increasing concentrations of the drug. Thes
Glycyl-tRNA synthetase (GARS) is one of 37 nuclear encoded amino acyl tRNA synthetases that function to attach amino acids onto their respective tRNA for protein translation.44 Since the discovery of GARS as a cause of dHMNV and CMT2D, mutations in three other amino acyl tRNAs have been identified as causes of intermediate CMT (DI-CMTC) (YARS, tyrosyl-tRNA synthetase),45 CMT2N (AARS, alanyl-tRNA synthetase)46 and autosomal recessive CMT2 (RI-CMTB) (KARS, lysyl-tRNA synthetase).47. In 2003, four different GARS mutations were discovered in five families with upper-limb predominant distal motor neuropathy (dHMNV or CMT2D).10 Six additional familial and sporadic cases of dHMN owing to GARS mutations have been reported.48-51 In an extended phenotype/genotype study of the original five families, 75% of affected family members presented in the second decade of life, with the majority functioning independently 40 years after disease onset.52 In one patient, weakness began in the lower limbs, ...
ID SYFB_BURP1 Reviewed; 810 AA. AC Q3JT07; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255,HAMAP-Rule:MF_00283}; DE EC=6.1.1.20 {ECO:0000255,HAMAP-Rule:MF_00283}; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255,HAMAP-Rule:MF_00283}; DE Short=PheRS {ECO:0000255,HAMAP-Rule:MF_00283}; GN Name=pheT {ECO:0000255,HAMAP-Rule:MF_00283}; GN OrderedLocusNames=BURPS1710b_1896; OS Burkholderia pseudomallei (strain 1710b). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320372; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1710b; RA Woods D.E., Nierman W.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). ...
Transfer ribonucleic acid1 is methylated after the molecule is synthesized; at least eight enzymes are involved in the transfer of methyl groups (derived from methionine). The time courses of methylation and synthesis of tRNA during rat liver regeneration have been compared in an in vivo radioisotopic study, using 6-orotic acid-14C and 3H-methyl-L-methionine as precursors in double label pulses. Liver regeneration is a synchronized system in which biochemical events of the cell cycle are separable. Transfer RNA methylation increase precedes by several hours tRNA synthesis during regeneration, although the curves overlap. A ratio of the relative rate of methylation to the relative rate of synthesis has been made; that curve positively correlates with the rise and fall of protein synthesis during regeneration. It is clear that methylation and synthesis of tRNA are only weakly coupled; changing methyl content of the tRNA "pool" resulting from differential tRNA methylase and polymerase activities ...

pars-2 - Prolyl Amino-acyl tRNA Synthetase - Caenorhabditis elegans - pars-2 gene & proteinpars-2 - Prolyl Amino-acyl tRNA Synthetase - Caenorhabditis elegans - pars-2 gene & protein

Prolyl Amino-acyl tRNA SynthetaseImported. ,p>Information which has been imported from another database using automatic ... tr,O45869,O45869_CAEEL Prolyl Amino-acyl tRNA Synthetase OS=Caenorhabditis elegans GN=pars-2 PE=1 SV=1 ... Aminoacyl-tRNA synthetaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p ... IPR002314. aa-tRNA-synt_IIb. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR036621. Anticodon-bd_dom_sf. IPR002316. ...
more infohttp://www.uniprot.org/uniprot/O45869

cars-1 - Cysteinyl Amino-acyl tRNA Synthetase - Caenorhabditis elegans - cars-1 gene & proteincars-1 - Cysteinyl Amino-acyl tRNA Synthetase - Caenorhabditis elegans - cars-1 gene & protein

Cysteinyl Amino-acyl tRNA SynthetaseImported. ,p>Information which has been imported from another database using automatic ... tr,A0A061ACL3,A0A061ACL3_CAEEL Cysteinyl Amino-acyl tRNA Synthetase OS=Caenorhabditis elegans OX=6239 GN=cars-1 PE=1 SV=1 ... Aminoacyl-tRNA synthetaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p ... IPR015803 Cys-tRNA-ligase. IPR024909 Cys-tRNA/MSH_ligase. IPR032678 tRNA-synt_1_cat_dom. IPR009080 tRNAsynth_Ia_anticodon-bd. ...
more infohttps://www.uniprot.org/uniprot/A0A061ACL3

Aminoacyl tRNA synthetase - WikipediaAminoacyl tRNA synthetase - Wikipedia

Amino+Acyl-tRNA+Synthetases at the US National Library of Medicine Medical Subject Headings (MeSH) ... "Aminoacyl-tRNA synthetases". Structural Biology. 5: 48-55.. *^ "Molecule of the Month: Aminoacyl-tRNA Synthetases High Fidelity ... An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto ... Amino Acid + tRNA + ATP → Aminoacyl-tRNA + AMP + PPi. Some synthetases also mediate an editing reaction to ensure high fidelity ...
more infohttps://en.wikipedia.org/wiki/Aminoacyl_tRNA_synthetase

Mitochondrial aminoacyl-tRNA synthetases in human disease.  - PubMed - NCBIMitochondrial aminoacyl-tRNA synthetases in human disease. - PubMed - NCBI

Amino Acyl-tRNA Synthetases/genetics*. *Amino Acyl-tRNA Synthetases/metabolism. *Brain Diseases, Metabolic/enzymology ... Mitochondrial aminoacyl-tRNA synthetases in human disease.. Konovalova S1, Tyynismaa H. ... Mitochondrial aminoacyl-tRNA synthetases (mtARSs) are essential in the process of transferring genetic information from ... These synthetases perform an integral step in the initiation of mitochondrial protein synthesis by charging tRNAs with their ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/23433712?dopt=Abstract

Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria.  - PubMed - NCBIImport of tRNAs and aminoacyl-tRNA synthetases into mitochondria. - PubMed - NCBI

Amino Acyl-tRNA Synthetases/genetics. *Amino Acyl-tRNA Synthetases/metabolism*. *Biological Transport/genetics ... Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria.. Duchêne AM1, Pujol C, Maréchal-Drouard L. ... All mitochondrial aminoacyl-tRNA synthetases and many tRNAs are imported from the cytosol into the mitochondria in eukaryotic ... Two crucial partners of the mitochondrial translation machinery are the aminoacyl-tRNA synthetases and the tRNAs. ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/19083240?dopt=Abstract

Synthetic Microcin C Analogs Targeting Different Aminoacyl-tRNA Synthetases | Journal of BacteriologySynthetic Microcin C Analogs Targeting Different Aminoacyl-tRNA Synthetases | Journal of Bacteriology

First, the N-acyl O-aminopropylphosphoramidate linker of the aspartyl-adenylate moiety of processed McC (compound 2) was ... Aminoacyl-tRNA synthetases (aaRSs) carry out the condensation of genetically encoded amino acids with cognate tRNAs. When 1 of ... Synthetic Microcin C Analogs Targeting Different Aminoacyl-tRNA Synthetases. Pieter Van de Vijver, Gaston H. M. Vondenhoff, ... Synthetic Microcin C Analogs Targeting Different Aminoacyl-tRNA Synthetases. Pieter Van de Vijver, Gaston H. M. Vondenhoff, ...
more infohttps://jb.asm.org/content/191/20/6273?ijkey=4999336c8d9a69eb5ce7e1e67c1c4d7de4ac097c&keytype2=tf_ipsecsha

aminoacyl tRNA synthetase p18 component
     Summary Report | CureHunteraminoacyl tRNA synthetase p18 component Summary Report | CureHunter

aminoacyl tRNA synthetase p18 component: shares a protein motif with the beta and gamma subunits of eukaryotic elongation ... factor 1; amino acid sequence given in first source ... Amino Acyl-tRNA Synthetases: 128*aminoacyl tRNA synthetase p18 ... aminoacyl tRNA synthetase p18 component. Subscribe to New Research on aminoacyl tRNA synthetase p18 component ... shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1; amino acid sequence given in first ...
more infohttp://www.curehunter.com/public/keywordSummaryC101946-aminoacyl-tRNA-synthetase-p18-component.do

Codon usage, amino acid usage, transfer RNA and amino-acyl-tRNA synthetases in mimiviruses - PAR00011189 - HorizonCodon usage, amino acid usage, transfer RNA and amino-acyl-tRNA synthetases in mimiviruses - PAR00011189 - Horizon

... tRNA) and amino acyl-tRNA synthetases. We confirmed that the codon and amino acid usages of these giant viruses are highly ... Codon usage, amino acid usage, transfer RNA and amino-acyl-tRNA synthetases in mimiviruses ... We further describe that the set of tRNAs and amino acyl-tRNA synthetases in mimiviruses is globally not adapted to the codon ... Colson P., Fournous G., Diene S. M., Raoult Didier. (2013). Codon usage, amino acid usage, transfer RNA and amino-acyl-tRNA ...
more infohttp://www.documentation.ird.fr/hor/PAR00011189

Aminoacyl-tRNA synthetases | definition of aminoacyl-tRNA synthetases by Medical dictionaryAminoacyl-tRNA synthetases | definition of aminoacyl-tRNA synthetases by Medical dictionary

What is aminoacyl-tRNA synthetases? Meaning of aminoacyl-tRNA synthetases medical term. What does aminoacyl-tRNA synthetases ... Looking for online definition of aminoacyl-tRNA synthetases in the Medical Dictionary? aminoacyl-tRNA synthetases explanation ... aminoacyl-tRNA synthetases. Also found in: Dictionary, Thesaurus. a·mi·no·ac·yl-tRNA syn·the·tas·es. enzymes catalyzing the ... aminoacyl-tRNA. transfer RNA to which its specific amino acid has been coupled by its specific aminoacyl-tRNA synthetase. ...
more infohttps://medical-dictionary.thefreedictionary.com/aminoacyl-tRNA+synthetases

Predicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis | Biology Direct | Full TextPredicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis | Biology Direct | Full Text

acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase. New_papain: novel family of papain-like cysteine proteases - ... tyrosine-tRNA synthetase. WTRS: tryptophan-tRNA synthetase. Gene and protein abbreviations: 2OGFEDO: 2-oxoglutarate and iron(II ... The least studied of these systems are those utilizing tRNAs or aminoacyl-tRNA synthetases (AAtRS) in non-ribosomal peptide ... tRNAs charged with the cognate amino acids by lysyl- or alanyl-tRNA synthetases are used by bacterial enzymes typified by ...
more infohttps://biologydirect.biomedcentral.com/articles/10.1186/1745-6150-5-48

MEDLINE - Resultado p gina 1
	MEDLINE - Resultado p gina 1

0 (Multiprotein Complexes); 9014-25-9 (RNA, Transfer); EC 6.1.1.- (Amino Acyl-tRNA Synthetases). ... Survey of the transcriptome suggests recognition of the mitochondrial tRNA-Met by the cytoplasmic aminoacyl-tRNA synthetase ... Aminoacil-tRNA Sintetases/gen tica. Animais. Sequ ncia de Bases. Cubomedusas/metabolismo. Regula o da Express o G nica. Genes ... counterpart and C-to-U editing of the cytoplasmic tRNA-Trp after import into the mitochondrion. Moreover, several mitochondrial ...
more infohttp://bases.bireme.br/cgi-bin/wxislind.exe/iah/online/?IsisScript=iah/iah.xis&nextAction=lnk&base=MEDLINE&lang=p&format=detailed.pft&indexSearch=EX&exprSearch=B01.050.500.308.361

Office of Science OutreachOffice of Science Outreach

tRNA-charging. Amino acyl-tRNA Synthetases carry out a two-step reaction involving ATP.. ...
more infohttp://www.indiana.edu/~oso/animations/An6.html

Plus itPlus it

... and amino acyl-tRNA synthetases (Mirande et al., 1985). eEF1A has been shown to colocalize with actin filaments in maize ... 1985) Association of an amino-acyl-transfer RNA synthetase complex and of phenylalanyl-transfer RNA synthetase with the ...
more infohttp://www.plantphysiol.org/content/116/4/1227

Methods for monitoring and measurement of protein translation in time and space  - Molecular BioSystems (RSC Publishing) DOI:10...Methods for monitoring and measurement of protein translation in time and space - Molecular BioSystems (RSC Publishing) DOI:10...

... achieved via co-expression of an orthogonal amino acyl-tRNA synthetase/tRNA pair in specific cells. The pyrrolysyl-tRNA ... Amino acyl-tRNA synthetase: a family of enzymes which catalyze the covalent conjugation of specific amino acids to their ... bacterial amino acyl-tRNA synthetases have been engineered to have a higher affinity for given non-canonical amino acids, and ... due to the permissive nature of certain amino acyl-tRNA synthetases. After incorporation, these amino acids can be either ...
more infohttp://pubs.rsc.org/en/content/articlehtml/2017/mb/c7mb00476a

Purification of each component used in the reconstitute | Open-iPurification of each component used in the reconstitute | Open-i

Amino Acyl-tRNA Synthetases/metabolism. *Binding Sites. *Cell-Free System. *DNA, Complementary/metabolism ... tRNAs. tRNAs (2 μg) were resolved by 8 m urea PAGE (12.5%) and stained with toluidine blue (TB). C, translation factors. eEF1s ... tRNAs. tRNAs (2 μg) were resolved by 8 m urea PAGE (12.5%) and stained with toluidine blue (TB). C, translation factors. eEF1s ... 4). These components were combined in a test tube with amino acids, triphosphate nucleotides (ATP, GTP, CTP, and UTP), and T7 ...
more infohttps://openi.nlm.nih.gov/detailedresult.php?img=PMC4231674_zbc0491400990004&req=4

Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like...Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like...

Amino Acid Sequence. MESH. Amino Acyl-tRNA Synthetases/metabolism. MESH. Binding Sites. MESH. ... Common ancestry of the regulatory HisZ subunit and class II aminoacyl-tRNA synthetase may reflect the balanced need of ... the structure of the regulatory HisZ subunit is distantly related to class II aminoacyl-tRNA synthetases. However, neither the ... Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like ...
more infohttps://epub.uni-regensburg.de/13678/

Frontiers | Saudi Moumouvirus, the First Group B Mimivirus Isolated from Asia | MicrobiologyFrontiers | Saudi Moumouvirus, the First Group B Mimivirus Isolated from Asia | Microbiology

The SDMV genome was predicted to encode 868 ORFs, ranging in size from 54 to 2,914 amino acids, with a mean size of 349 aa. ... The SDMV genome was predicted to encode 868 ORFs, ranging in size from 54 to 2,914 amino acids, with a mean size of 349 aa. ... transfer RNA and amino-acyl-tRNA synthetases in Mimiviruses. Intervirology 56, 364-375. doi: 10.1159/000354557 ... we observed an unusual set of aminoacyl-tRNA synthetase (aaRS), which are translation-related genes not found in viruses other ...
more infohttps://www.frontiersin.org/articles/10.3389/fmicb.2016.02029/full

Ted M Dawson - Research Output
     - Johns Hopkins UniversityTed M Dawson - Research Output - Johns Hopkins University

Amino Acyl-tRNA Synthetases PINK1-dependent recruitment of Parkin to mitochondria in mitophagy. Vives-Bauza, C., Zhou, C., ...
more infohttps://jhu.pure.elsevier.com/en/persons/ted-m-dawson/publications/?page=3

Neil McHugh - Research Output
     - the University of Baths research portalNeil McHugh - Research Output - the University of Bath's research portal

Amino Acyl-tRNA Synthetases Polymyositis Interstitial Lung Diseases Ligases Autoantibodies Anti-topoisomerase I antibodies in ... Anti-synthetase syndrome: a new autoantibody to phenylalanyl transfer RNA synthetase (anti-Zo) associated with polymyositis and ...
more infohttps://researchportal.bath.ac.uk/en/persons/neil-mchugh/publications/?ordering=type&descending=false

Investigation of myositis and scleroderma specific autoantibodies in patients with lung cancer<...Investigation of myositis and scleroderma specific autoantibodies in patients with lung cancer<...

Amino Acyl-tRNA Synthetases Connective Tissue Diseases Dermatomyositis Small Cell Lung Carcinoma ... Anti-glycyl-transfer RNA (tRNA) synthetase (anti-EJ) autoantibodies were detected in one patient with non-small cell lung ... Anti-glycyl-transfer RNA (tRNA) synthetase (anti-EJ) autoantibodies were detected in one patient with non-small cell lung ... Anti-glycyl-transfer RNA (tRNA) synthetase (anti-EJ) autoantibodies were detected in one patient with non-small cell lung ...
more infohttps://researchportal.bath.ac.uk/en/publications/investigation-of-myositis-and-scleroderma-specific-autoantibodies

Life  | Free Full-Text | Is Research on Synthetic Cells Moving to the Next Level? | HTMLLife | Free Full-Text | Is Research on "Synthetic Cells" Moving to the Next Level? | HTML

36 proteins (20 amino acyl-tRNA synthetase, 10 translation factors, 4 energy-related enzymes, T7 RNA polymerase, methionine ... Hong, S.H.; Kwon, Y.-C.; Jewett, M.C. Non-standard amino acid incorporation into proteins using Escherichia coli cell-free ... Dong, H.; Nilsson, L.; Kurland, C.G. Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth ...
more infohttps://www.mdpi.com/2075-1729/9/1/3/htm

HF interacts with both the site for amino acid activati | Open-iHF interacts with both the site for amino acid activati | Open-i

HF interacts with both the site for amino acid activation and the site for docking the 3′-end of tRNAa, Thermal melting19 of ... Amino Acyl-tRNA Synthetases/antagonists & inhibitors/chemistry*/metabolism*. *Piperidines/chemistry*/metabolism*/pharmacology ... ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. ... ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. ...
more infohttps://openi.nlm.nih.gov/detailedresult.php?img=PMC3569068_nihms-420657-f0003&req=4

WO2011139714A2 - Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of...WO2011139714A2 - Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of...

Provided are compositions comprising newly identified protein fragments of aminoacyl-tRNA synthetases, polynucleotides that ... 108010078698 Amino Acyl-tRNA Synthetases Proteins 0 abstract claims description 239 * 229920000023 polynucleotides Polymers 0 ... 102000014745 Amino Acyl-tRNA Synthetases Human genes 0 abstract claims description 186 ... 229940019746 Antifibrinolytic amino acids Drugs 0 description 89 * 229940021015 I.V. solution additive Amino Acids Drugs 0 ...
more infohttps://patents.google.com/patent/WO2011139714A2/en

The significance of translation regulation in the stress response | BMC Genomics | Full TextThe significance of translation regulation in the stress response | BMC Genomics | Full Text

... and amino acyl tRNA synthetases (AspS, LeuS, LysS, MetS, PheT, ProS, ThrS and TrpS). The genes for RpsS, PepP and PrfC were in ... and amino acyl tRNA synthetases (alaS, aspS, hisS, leuS, lysS, pheS, pheT, proS, thrS and valS)], transcription [genes related ... translation factors and amino acyl tRNA synthetases. We have demonstrated here that these genes were down-regulated, at the ... Under a low availability of an amino acid, higher density could result from ribosome congestion near the codons of this amino ...
more infohttps://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-14-588
  • The identified mutation spectrum suggests that only mutation types that allow some residual tRNA-charging activity can result in the described mtARS diseases but the molecular mechanisms behind the selective tissue involvement are not currently understood. (nih.gov)
  • In contrast, glycine- and L-amino acid-containing cross-links are synthesized by the Fem ligases of the GCN5-like acetyltransferase (GNAT) fold. (biomedcentral.com)
  • Notwithstanding, Leu(TAA)tRNA, present in several Mimivirus genomes and in multiple copies in some viral genomes, may complement the amoebal tRNA pool and may contribute to accommodate the viral AT-rich codons. (ird.fr)
  • We confirmed that the codon and amino acid usages of these giant viruses are highly dissimilar to those in their amoebal host Acanthamoeba castellanii and are instead correlated with the high adenine and thymine (AT) content of Mimivirus genomes. (ird.fr)
  • Regardless of where the aminoacyl is initially attached to the nucleotide, the 2'- O -aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification . (wikipedia.org)