Stereochemical mechanisms of tRNA methyltransferases

被引:35
作者
Hou, Ya-Ming [1 ]
Perona, John J. [2 ]
机构
[1] Thomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USA
[2] Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA
关键词
S-adenosylmethionine; SAM-dependent methyl transfer; Rossmann-fold; Methylase; TrmA; Trm5; ESCHERICHIA-COLI ENCODES; YEAST TRANSFER-RNA; CRYSTAL-STRUCTURE; M(7)G46 METHYLTRANSFERASE; SACCHAROMYCES-CEREVISIAE; MODIFIED NUCLEOSIDES; DEPENDENT METHYLTRANSFERASE; DNA METHYLTRANSFERASE; SUBSTRATE SELECTIVITY; CATALYTIC EFFICIENCY;
D O I
10.1016/j.febslet.2009.11.075
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Methylation of tRNA on the four canonical bases adds structural complexity to the molecule, and improves decoding specificity and efficiency. While many tRNA methylases are known, detailed insight into the catalytic mechanism is only available in a few cases. Of interest among all tRNA methylases is the structural basis for nucleotide selection, by which the specificity is limited to a single site, or broadened to multiple sites. General themes in catalysis include the basis for rate acceleration at highly diverse nucleophilic centers for methyl transfer, using S-adenosylmethionine as a cofactor. Studies of tRNA methylases have also yielded insights into molecular evolution, particularly in the case of enzymes that recognize distinct structures to perform identical reactions at the same target nucleotide. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:278 / 286
页数:9
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