RRC ID 53703
著者 Kim J, Xiao H, Koh J, Wang Y, Bonanno JB, Thomas K, Babbitt PC, Brown S, Lee YS, Almo SC.
タイトル Determinants of the CmoB carboxymethyl transferase utilized for selective tRNA wobble modification.
ジャーナル Nucleic Acids Res
Abstract Enzyme-mediated modifications at the wobble position of tRNAs are essential for the translation of the genetic code. We report the genetic, biochemical and structural characterization of CmoB, the enzyme that recognizes the unique metabolite carboxy-S-adenosine-L-methionine (Cx-SAM) and catalyzes a carboxymethyl transfer reaction resulting in formation of 5-oxyacetyluridine at the wobble position of tRNAs. CmoB is distinctive in that it is the only known member of the SAM-dependent methyltransferase (SDMT) superfamily that utilizes a naturally occurring SAM analog as the alkyl donor to fulfill a biologically meaningful function. Biochemical and genetic studies define the in vitro and in vivo selectivity for Cx-SAM as alkyl donor over the vastly more abundant SAM. Complementary high-resolution structures of the apo- and Cx-SAM bound CmoB reveal the determinants responsible for this remarkable discrimination. Together, these studies provide mechanistic insight into the enzymatic and non-enzymatic feature of this alkyl transfer reaction which affords the broadened specificity required for tRNAs to recognize multiple synonymous codons.
巻・号 43(9)
ページ 4602-13
公開日 2015-5-19
DOI 10.1093/nar/gkv206
PII gkv206
PMID 25855808
PMC PMC4482062
MeSH Binding Sites Escherichia coli Proteins / chemistry* Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism Ligands Methyltransferases / chemistry* Methyltransferases / genetics Methyltransferases / metabolism Mutation RNA, Transfer / chemistry RNA, Transfer / metabolism* S-Adenosylmethionine / analogs & derivatives* S-Adenosylmethionine / chemistry Thermodynamics
IF 11.502
引用数 9
リソース情報
原核生物(大腸菌)