Transfer RNAs (tRNAs) enter ribosome-mediated protein biosynthesis in a translationally competent state, which includes post-transcriptional modifications at various positions, including the anticodon loop, and the presence of an intact single-stranded CCA-sequence at the 3′-terminus that is required for amino acid attachment by the corresponding aminoacyl-tRNA-synthetase [7] . (prolekarniky.cz)
Transfer RNAs (tRNAs) maintain translation fidelity through accurate charging by their cognate aminoacyl-tRNA synthetase and codon:anticodon base pairing with the mRNA at the ribosome. (bvsalud.org)
Ubiquitin ligase1
Moreover, we observed that PUS10 is ubiquitinated by E3 ubiquitin ligase CRL4DCAF1 complex and the increase of PUS10 in aged HSPC is due to aging-declined CRL4DCAF1- mediated ubiquitination degradation signaling. (haematologica.org)
Enzyme10
In enzymology, a methionine-tRNA ligase (EC 6.1.1.10) is an enzyme that catalyzes the chemical reaction ATP + L-methionine + tRNAMet ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-methionyl-tRNAMet The 3 substrates of this enzyme are ATP, L-methionine, and tRNA(Met), whereas its 3 products are AMP, diphosphate, and L-methionyl-tRNA(Met). (wikipedia.org)
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. (wikipedia.org)
The systematic name of this enzyme class is L-methionine:tRNAMet ligase (AMP-forming). (wikipedia.org)
This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid metabolism, and aminoacyl-trna biosynthesis. (wikipedia.org)
During oxidative stress, methionine-tRNA ligase might be phosphorylated, which results in promiscuity of this enzyme, where it aminoacylates methionine to various non-Met tRNAs. (wikipedia.org)
This CCA deactivation is reversible and quickly repairable by the CCA-adding enzyme [ATP(CTP):tRNA nucleotidyltransferase]. (prolekarniky.cz)
Some bacteria carry tRNA genes encoding CCA termini, thus the CCA-adding enzyme is primarily involved in repairing damaged CCA ends in these organisms [9] . (prolekarniky.cz)
The functional repertoire of the CCA-adding enzyme has been expanded by its recently discovered role in the quality control of hypo-modified tRNAs [12] . (prolekarniky.cz)
Thereby, two tRNA-halves (designated 5′- and 3′-tiRNAs) are generated by a ubiquitously expressed enzyme, angiogenin [18] . (prolekarniky.cz)
Fumagillin can block blood vessel formation by binding to an enzyme methionine aminopeptidase and for this reason, the compound, together with semisynthetic derivatives, are investigated as an angiogenesis inhibitor in the treatment of cancer. (xcessbio.com)
Predicted to be involved in isoleucyl-tRNA aminoacylation and mitochondrial translation. (mcw.edu)
Oxidative stress3
This in turn leads to substitution of amino acids in proteins with methionine, which helps relieve oxidative stress in the cell. (wikipedia.org)
In this study, we demonstrate that exposure to oxidative stress results in a quick repression of translation by deactivation of the aminoacyl-ends of all transfer-RNA (tRNA). (prolekarniky.cz)
An oxidative-stress activated nuclease, angiogenin, cleaves first within the conserved single-stranded 3′-CCA termini of all tRNAs, thereby blocking their use in translation. (prolekarniky.cz)
Subsp1
Crystal structure of arginyl-tRNA synthetase from Klebsiella pneumoniae subsp. (embl-heidelberg.de)
Protein2
Click on the protein counts, or double click on taxonomic names to display all proteins containing Arg_tRNA_synt_N domain in the selected taxonomic class. (embl-heidelberg.de)
42520) hypothetical protein CP001857 tRNA Arcpr_R0002 complement(42639. (go.jp)
Proteins5
There are 26085 Arg_tRNA_synt_N domains in 26083 proteins in SMART's nrdb database. (embl-heidelberg.de)
Taxonomic distribution of proteins containing Arg_tRNA_synt_N domain. (embl-heidelberg.de)
The complete taxonomic breakdown of all proteins with Arg_tRNA_synt_N domain is also avaliable . (embl-heidelberg.de)
Starting with a degron: N-terminal formyl-methionine of nascent bacterial proteins contributes to their proteolytic control. (microbialcell.com)
In bacteria, all nascent proteins bear the pretranslationally formed N-terminal formyl-methionine (fMet) residue. (microbialcell.com)
Methionyl2
Other names in common use include methionyl-tRNA synthetase, methionyl-transfer ribonucleic acid synthetase, methionyl-transfer ribonucleate synthetase, methionyl-transfer RNA synthetase, methionine translase, and MetRS. (wikipedia.org)
The endonucleolytic tRNA cleavage is a conserved feature in higher eukaryotes. (prolekarniky.cz)
The degron-binding pockets and specific pocket residues implicated in Ala-tail recognition are conserved among Pirh2 and KLHDC10 homologs, suggesting that an important function of these ligases across eukaryotes is in targeting Ala-tailed substrates. (bvsalud.org)
tRNA synthetase class II core domain (G, Seryl-tRNA synthetase N-terminal domain [Interproscan]. (ntu.edu.sg)
Amino1
This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). (embl-heidelberg.de)
Alanine2
In order to prove the non-involvement of the axial ligand, a subsequent double mutant (C14A/M69A) was constructed, replacing the methionine at 69 position with non-coordinating alanine residue. (bvsalud.org)
Further improvement in the reconstitution process is achieved by replacing the methionine at 69 position with phenyl alanine (C14A/M69F mutant), resulting in further stabilization of heme species, possibly through non-covalent π-interactions, as corroborated by molecular docking. (bvsalud.org)
Recognition1
It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition. (embl-heidelberg.de)
Enzymes1
While all cancers with ALD confirm enzymes in the Typical download volatility, there is no spermatogonial hypothalamus methionine. (evakoch.com)
Class2
However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. (embl-heidelberg.de)
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. (embl-heidelberg.de)
Domain1
In ribosome-associated quality control (RQC), nascent polypeptides produced by interrupted translation are modified with C-terminal polyalanine tails ("Ala-tails") that function outside ribosomes to induce ubiquitylation by E3 ligases Pirh2 (p53-induced RING-H2 domain-containing) or CRL2 (Cullin-2 RING ligase2)-KLHDC10. (bvsalud.org)
Translation1
This cleavage, however, does not significantly reduce the level of mature tRNAs, which implies that tiRNAs may rather act as a signal transducer to modulate translation of specific mRNAs, than to globally repress translation [18] . (prolekarniky.cz)
Growth1
Mature, translationally competent tRNAs are very stable under normal growth conditions, with a half-life of approximately one to several hours [13] . (prolekarniky.cz)
Active1
FIDAS-5 is a potent and orally active methionine S-adenosyltransferase 2A (MAT2A) inhibitor with an IC50 of 2.1 μM. (xcessbio.com)
Methionyl-tRNA3
This gene produces a mitochondrial methionyl-tRNA synthetase protein that is encoded by the nuclear genome and imported to the mitochondrion. (nih.gov)
In enzymology, a methionine-tRNA ligase (EC 6.1.1.10) is an enzyme that catalyzes the chemical reaction ATP + L-methionine + tRNAMet ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-methionyl-tRNAMet The 3 substrates of this enzyme are ATP, L-methionine, and tRNA(Met), whereas its 3 products are AMP, diphosphate, and L-methionyl-tRNA(Met). (wikipedia.org)
Other names in common use include methionyl-tRNA synthetase, methionyl-transfer ribonucleic acid synthetase, methionyl-transfer ribonucleate synthetase, methionyl-transfer RNA synthetase, methionine translase, and MetRS. (wikipedia.org)
Ubiquitin1
GTBP Mutations in the ubiquitin E3 ligase, create a lack of E3 ligase activity3C5. (monossabios.com)
Incubation of either reagent with IleRS resulted in a rapid loss of both the tRNA Ile aminoacylation and isoleucinedependent isotopic ATP-PPi exchange activities. (openbiochemistryjournal.com)