Functional Characterization of the YmcB and YqeV tRNA Methylthiotransferases of Bacillus Subtilis

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dc.contributor.author Anton, Brian P. en_US
dc.contributor.author Russell, Susan P. en_US
dc.contributor.author Vertrees, Jason en_US
dc.contributor.author Kasif, Simon en_US
dc.contributor.author Raleigh, Elisabeth A. en_US
dc.contributor.author Limbach, Patrick A. en_US
dc.contributor.author Roberts, Richard J. en_US
dc.date.accessioned 2012-01-11T00:40:39Z
dc.date.available 2012-01-11T00:40:39Z
dc.date.copyright 2010 en_US
dc.date.issued 2010-5-14 en_US
dc.identifier.citation Anton, Brian P., Susan P. Russell, Jason Vertrees, Simon Kasif, Elisabeth A. Raleigh, Patrick A. Limbach, Richard J. Roberts. "Functional characterization of the YmcB and YqeV tRNA methylthiotransferases of Bacillus subtilis" Nucleic Acids Research 38(18): 6195-6205. (2010) en_US
dc.identifier.issn 1362-4962 en_US
dc.identifier.uri http://hdl.handle.net/2144/3033
dc.description.abstract Methylthiotransferases (MTTases) are a closely related family of proteins that perform both radical-S-adenosylmethionine (SAM) mediated sulfur insertion and SAM-dependent methylation to modify nucleic acid or protein targets with a methyl thioether group (–SCH3). Members of two of the four known subgroups of MTTases have been characterized, typified by MiaB, which modifies N6-isopentenyladenosine (i6A) to 2-methylthio-N6-isopentenyladenosine (ms2i6A) in tRNA, and RimO, which modifies a specific aspartate residue in ribosomal protein S12. In this work, we have characterized the two MTTases encoded by Bacillus subtilis 168 and find that, consistent with bioinformatic predictions, ymcB is required for ms2i6A formation (MiaB activity), and yqeV is required for modification of N6-threonylcarbamoyladenosine (t6A) to 2-methylthio-N6-threonylcarbamoyladenosine (ms2t6A) in tRNA. The enzyme responsible for the latter activity belongs to a third MTTase subgroup, no member of which has previously been characterized. We performed domain-swapping experiments between YmcB and YqeV to narrow down the protein domain(s) responsible for distinguishing i6A from t6A and found that the C-terminal TRAM domain, putatively involved with RNA binding, is likely not involved with this discrimination. Finally, we performed a computational analysis to identify candidate residues outside the TRAM domain that may be involved with substrate recognition. These residues represent interesting targets for further analysis. en_US
dc.description.sponsorship National Science Foundation (CHE 0602413, CHE 0910751); National Institutes of Health (NIH RR019900); National Institutes of Health (NIH 1RC2GM092602-01) en_US
dc.language.iso en en_US
dc.rights Copyright Anton, Brian P., Susan P. Russell, Jason Vertrees, Simon Kasif, Elisabeth A. Raleigh, Patrick A. Limbach, Richard J. Roberts2010. Published by Oxford University Press. en_US
dc.rights.uri http://creativecommons.org/licenses/by-nc/2.5 en_US
dc.title Functional Characterization of the YmcB and YqeV tRNA Methylthiotransferases of Bacillus Subtilis en_US
dc.type article en_US
dc.identifier.doi 10.1093/nar/gkq364 en_US
dc.identifier.pubmedid 20472640 en_US
dc.identifier.pmcid 2952846 en_US

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