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tRNA modification enzymes GidA and MnmE: potential role in virulence of bacterial pathogens.
Shippy DC, Fadl AA. Shippy DC, et al. Int J Mol Sci. 2014 Oct 10;15(10):18267-80. doi: 10.3390/ijms151018267. Int J Mol Sci. 2014. PMID: 25310651 Free PMC article. Review.
Transfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. ...Many enzymes have been implicated in the modification of bacterial tRNAs, and these enzymes may complex with one another or interact individually
Transfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. ...Many
GidA, a tRNA Modification Enzyme, Contributes to the Growth, and Virulence of Streptococcus suis Serotype 2.
Gao T, Tan M, Liu W, Zhang C, Zhang T, Zheng L, Zhu J, Li L, Zhou R. Gao T, et al. Front Cell Infect Microbiol. 2016 Apr 19;6:44. doi: 10.3389/fcimb.2016.00044. eCollection 2016. Front Cell Infect Microbiol. 2016. PMID: 27148493 Free PMC article.
Glucose-inhibited division protein (GidA), is a tRNA modification enzyme functioning together with MnmE in the addition of a carboxymethylaminomethyl group to position 5 of the anticodon wobble uridine of tRNA. Here, we report a GidA homolog from a Chi …
Glucose-inhibited division protein (GidA), is a tRNA modification enzyme functioning together with MnmE in the addition of a c …
Bacillus subtilis exhibits MnmC-like tRNA modification activities.
Moukadiri I, Villarroya M, Benítez-Páez A, Armengod ME. Moukadiri I, et al. RNA Biol. 2018;15(9):1167-1173. doi: 10.1080/15476286.2018.1517012. Epub 2018 Sep 24. RNA Biol. 2018. PMID: 30249152 Free PMC article.
The MnmE-MnmG complex of Escherichia coli uses either ammonium or glycine as a substrate to incorporate the 5-aminomethyl or 5-carboxymethylaminomethyl group into the wobble uridine of certain tRNAs. ...The glycine pathway has been considered predominant in this typical gr …
The MnmE-MnmG complex of Escherichia coli uses either ammonium or glycine as a substrate to incorporate the 5-aminomethyl or 5-carbox …
SAXS analysis of the tRNA-modifying enzyme complex MnmE/MnmG reveals a novel interaction mode and GTP-induced oligomerization.
Fislage M, Brosens E, Deyaert E, Spilotros A, Pardon E, Loris R, Steyaert J, Garcia-Pino A, Versées W. Fislage M, et al. Nucleic Acids Res. 2014 May;42(9):5978-92. doi: 10.1093/nar/gku213. Epub 2014 Mar 14. Nucleic Acids Res. 2014. PMID: 24634441 Free PMC article.
Transfer ribonucleic acid (tRNA) modifications, especially at the wobble position, are crucial for proper and efficient protein translation. ...MnmE is a G protein activated by dimerization (GAD), and active guanosine-5'-triphosphate (GTP) hydrolysis is required for
Transfer ribonucleic acid (tRNA) modifications, especially at the wobble position, are crucial for proper and efficient protei
Virulence characteristics of Salmonella following deletion of genes encoding the tRNA modification enzymes GidA and MnmE.
Shippy DC, Eakley NM, Lauhon CT, Bochsler PN, Fadl AA. Shippy DC, et al. Microb Pathog. 2013 Apr;57:1-9. doi: 10.1016/j.micpath.2013.01.004. Epub 2013 Jan 29. Microb Pathog. 2013. PMID: 23375888
In Escherichia coli, GidA and MnmE have been shown to modify several bacterial factors by a post-transcriptional mechanism to modify tRNA. ...Overall, the data suggest MnmE and GidA bind together and use a post-transcriptional mechanism to modify tRNA
In Escherichia coli, GidA and MnmE have been shown to modify several bacterial factors by a post-transcriptional mechanism to modify …
Proteomic and Metabolomic Analyses Provide Insights into the Mechanism on Arginine Metabolism Regulated by tRNA Modification Enzymes GidA and MnmE of Streptococcus suis.
Gao T, Yuan F, Liu Z, Liu W, Zhou D, Yang K, Guo R, Liang W, Zou G, Zhou R, Tian Y. Gao T, et al. Front Cell Infect Microbiol. 2020 Dec 11;10:597408. doi: 10.3389/fcimb.2020.597408. eCollection 2020. Front Cell Infect Microbiol. 2020. PMID: 33425782 Free PMC article.
GidA and MnmE, two important tRNA modification enzymes, are contributed to the addition of the carboxymethylaminomethyl (cmnm) group onto wobble uridine of tRNA. ...However, its function remains poorly elucidated in zoonotic Streptococcus suis (SS). Here, a
GidA and MnmE, two important tRNA modification enzymes, are contributed to the addition of the carboxymethylaminomethyl (cmnm)
Further insights into the tRNA modification process controlled by proteins MnmE and GidA of Escherichia coli.
Yim L, Moukadiri I, Björk GR, Armengod ME. Yim L, et al. Nucleic Acids Res. 2006;34(20):5892-905. doi: 10.1093/nar/gkl752. Epub 2006 Oct 24. Nucleic Acids Res. 2006. PMID: 17062623 Free PMC article.
However, their precise role in the modification reaction remains undetermined. Here, we show that GidA is an FAD-binding protein and that mutagenesis of the N-terminal dinucleotide-binding motif of GidA, impairs capability of this protein to bind FAD and modify t
However, their precise role in the modification reaction remains undetermined. Here, we show that GidA is an FAD-binding protein and …
Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate.
Meyer S, Scrima A, Versées W, Wittinghofer A. Meyer S, et al. J Mol Biol. 2008 Jul 11;380(3):532-47. doi: 10.1016/j.jmb.2008.04.072. Epub 2008 May 7. J Mol Biol. 2008. PMID: 18565343
GidA is a flavin-adenine-dinucleotide (FAD)-binding protein that is conserved among bacteria and eucarya. ...Finally, a large patch of highly conserved, positively charged residues on the surface of GidA leading to the FAD-binding site suggests a tRNA-binding
GidA is a flavin-adenine-dinucleotide (FAD)-binding protein that is conserved among bacteria and eucarya. ...Finally, a large patch o
Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions.
Moukadiri I, Prado S, Piera J, Velázquez-Campoy A, Björk GR, Armengod ME. Moukadiri I, et al. Nucleic Acids Res. 2009 Nov;37(21):7177-93. doi: 10.1093/nar/gkp762. Nucleic Acids Res. 2009. PMID: 19767610 Free PMC article.
The lack of this tRNA modification produces a pleiotropic phenotype in bacteria and has been associated with mitochondrial encephalomyopathies in humans. ...In both reactions, methylene-tetrahydrofolate is the most probable source to form the C5-methylene moiety, whereas N …
The lack of this tRNA modification produces a pleiotropic phenotype in bacteria and has been associated with mitochondrial encephalom …
Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme.
Shi R, Villarroya M, Ruiz-Partida R, Li Y, Proteau A, Prado S, Moukadiri I, Benítez-Páez A, Lomas R, Wagner J, Matte A, Velázquez-Campoy A, Armengod ME, Cygler M. Shi R, et al. J Bacteriol. 2009 Dec;191(24):7614-9. doi: 10.1128/JB.00650-09. Epub 2009 Oct 2. J Bacteriol. 2009. PMID: 19801413 Free PMC article.
The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding an …
The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG
39 results