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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.
MnmE and MnmG, but not MnmC, are evolutionarily conserved. Bacillus subtilis lacks genes encoding MnmC(o) and/or MnmC(m) homologs. ...Our data indicate that B. subtilis has evolved MnmC(o)- and MnmC(m)-like activities that reside in non MnmC
MnmE and MnmG, but not MnmC, are evolutionarily conserved. Bacillus subtilis lacks genes encoding MnmC(o) and/or MnmC(m …
The output of the tRNA modification pathways controlled by the Escherichia coli MnmEG and MnmC enzymes depends on the growth conditions and the tRNA species.
Moukadiri I, Garzón MJ, Björk GR, Armengod ME. Moukadiri I, et al. Nucleic Acids Res. 2014 Feb;42(4):2602-23. doi: 10.1093/nar/gkt1228. Epub 2013 Nov 30. Nucleic Acids Res. 2014. PMID: 24293650 Free PMC article.
We demonstrate that the two MnmC domains function independently of each other and that tRNA(cmnm5s2UUG)(Gln) and tRNA(cmnm5UmAA)(Leu), are substrates for MnmC(m), but not MnmC(o). Synthesis of mnm(5)s(2)U by MnmEG-MnmC in vivo avoids buil …
We demonstrate that the two MnmC domains function independently of each other and that tRNA(cmnm5s2UUG)(Gln) and tRNA(c …
Enzymology of tRNA modification in the bacterial MnmEG pathway.
Armengod ME, Moukadiri I, Prado S, Ruiz-Partida R, Benítez-Páez A, Villarroya M, Lomas R, Garzón MJ, Martínez-Zamora A, Meseguer S, Navarro-González C. Armengod ME, et al. Biochimie. 2012 Jul;94(7):1510-20. doi: 10.1016/j.biochi.2012.02.019. Epub 2012 Feb 28. Biochimie. 2012. PMID: 22386868 Review.
Among all RNAs, tRNA exhibits the largest number and the widest variety of post-transcriptional modifications. ...While the IscS-MnmA pathway and the MnmA-mediated thiouridylation reaction are relatively well understood, we have limited information on the reactions mediate …
Among all RNAs, tRNA exhibits the largest number and the widest variety of post-transcriptional modifications. ...While the IscS-MnmA …
Biocatalytic Reversal of Advanced Glycation End Product Modification.
Kim NY, Goddard TN, Sohn S, Spiegel DA, Crawford JM. Kim NY, et al. Chembiochem. 2019 Sep 16;20(18):2402-2410. doi: 10.1002/cbic.201900158. Epub 2019 Aug 9. Chembiochem. 2019. PMID: 31013547 Free PMC article.
Despite a significant number of studies showing strong associations between AGEs and the pathologies of aging-related illnesses, it has been a challenge to establish AGEs as causal agents primarily due to the lack of tools in reversing AGE modifications at the molecular level. He …
Despite a significant number of studies showing strong associations between AGEs and the pathologies of aging-related illnesses, it has been …
Identification of a novel 5-aminomethyl-2-thiouridine methyltransferase in tRNA modification.
Cho G, Lee J, Kim J. Cho G, et al. Nucleic Acids Res. 2023 Feb 28;51(4):1971-1983. doi: 10.1093/nar/gkad048. Nucleic Acids Res. 2023. PMID: 36762482 Free PMC article.
The uridine at the 34th position of tRNA, which is able to base pair with the 3'-end codon on mRNA, is usually modified to influence many aspects of decoding properties during translation. ...Although mnm5s2U has been identified in tRNAs of Gram-positive bacteria and plant …
The uridine at the 34th position of tRNA, which is able to base pair with the 3'-end codon on mRNA, is usually modified to influence …
Crystal structure of the bifunctional tRNA modification enzyme MnmC from Escherichia coli.
Kitamura A, Sengoku T, Nishimoto M, Yokoyama S, Bessho Y. Kitamura A, et al. Protein Sci. 2011 Jul;20(7):1105-13. doi: 10.1002/pro.659. Epub 2011 Jun 2. Protein Sci. 2011. PMID: 21574198 Free PMC article.
Post-transcriptional modifications of bases within the transfer RNAs (tRNA) anticodon significantly affect the decoding system. ...The C-terminal domain of MnmC (MnmC1) is responsible for the flavin adenine dinucleotide (FAD)-dependent deacetylation of cmnm5U …
Post-transcriptional modifications of bases within the transfer RNAs (tRNA) anticodon significantly affect the decoding system …
Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC.
Kim J, Almo SC. Kim J, et al. BMC Struct Biol. 2013 Apr 24;13:5. doi: 10.1186/1472-6807-13-5. BMC Struct Biol. 2013. PMID: 23617613 Free PMC article.
RESULTS: The X-ray crystal structures of SAM/FAD-bound bifunctional MnmC from Escherichia coli and Yersinia pestis, and FAD-bound bifunctional MnmC from Yersinia pestis were determined and the catalytic functions verified in an in vitro assay. ...The structures of …
RESULTS: The X-ray crystal structures of SAM/FAD-bound bifunctional MnmC from Escherichia coli and Yersinia pestis, and FAD-bound bif …
Characterization and structure of the Aquifex aeolicus protein DUF752: a bacterial tRNA-methyltransferase (MnmC2) functioning without the usually fused oxidase domain (MnmC1).
Kitamura A, Nishimoto M, Sengoku T, Shibata R, Jäger G, Björk GR, Grosjean H, Yokoyama S, Bessho Y. Kitamura A, et al. J Biol Chem. 2012 Dec 21;287(52):43950-60. doi: 10.1074/jbc.M112.409300. Epub 2012 Oct 22. J Biol Chem. 2012. PMID: 23091054 Free PMC article.
Aquifex aeolicus lacks a bifunctional MnmC protein fusion and instead encodes the Rossmann-fold protein DUF752, which is homologous to the methyltransferase MnmC2 domain of Escherichia coli MnmC (26% identity). Here, we determined the crystal structure of the A. aeo …
Aquifex aeolicus lacks a bifunctional MnmC protein fusion and instead encodes the Rossmann-fold protein DUF752, which is homologous t …
Computational design of prospective molecular targets for Burkholderia cepacia complex by molecular docking and dynamic simulation studies.
Skariyachan S, Praveen PKU, Uttarkar A, Niranjan V. Skariyachan S, et al. Proteins. 2023 Jun;91(6):724-738. doi: 10.1002/prot.26462. Epub 2023 Jan 13. Proteins. 2023. PMID: 36601892
The study aimed to screen prospective molecular targets of BCC and potential natural lead candidates as effective binders by computational modeling, molecular docking, and dynamic (MD) simulation studies. Based on the virulent functions, tRNA 5-methylaminomethyl-2-thiourid …
The study aimed to screen prospective molecular targets of BCC and potential natural lead candidates as effective binders by computational m …
Assay of both activities of the bifunctional tRNA-modifying enzyme MnmC reveals a kinetic basis for selective full modification of cmnm5s2U to mnm5s2U.
Pearson D, Carell T. Pearson D, et al. Nucleic Acids Res. 2011 Jun;39(11):4818-26. doi: 10.1093/nar/gkr071. Epub 2011 Feb 8. Nucleic Acids Res. 2011. PMID: 21306992 Free PMC article.
Transfer RNA (tRNA) contains a number of complex 'hypermodified' nucleosides that are essential for a number of genetic processes. ...To investigate this concept, we measured steady-state kinetics for the final two steps of the biosynthesis of the mnm(5)s(2)U
Transfer RNA (tRNA) contains a number of complex 'hypermodified' nucleosides that are essential for a number of genetic
16 results