Functional analysis of the conserved histidine residue of Bamboo mosaic virus capping enzyme in the activity for the formation of the covalent enzyme-m7GMP intermediate

被引:8
|
作者
Lin, Hua-Yang [1 ]
Yu, Chiao-Yuan [1 ]
Hsu, Yau-Heiu [1 ]
Meng, Menghsiao [1 ]
机构
[1] Natl Chung Hsing Univ, Grad Inst Biotechnol, Taichung 40227, Taiwan
来源
FEBS LETTERS | 2012年 / 586卷 / 16期
关键词
Bamboo mosaic virus; Alphavirus-like superfamily; Hydroxylamine; Capping enzyme; Guanylyltransferase; VESICULAR STOMATITIS-VIRUS; SACCHAROMYCES-CEREVISIAE; DEPENDENT GUANYLYLTRANSFERASE; S-ADENOSYLMETHIONINE; NUCLEOTIDYL TRANSFER; RNA-POLYMERASE; PROTEIN; DOMAIN; SITE; METHYLTRANSFERASE;
D O I
10.1016/j.febslet.2012.05.024
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
The alphavirus-like mRNA capping enzyme of Bamboo mosaic virus (BaMV) exhibits an AdoMet-dependent guanylyltransferase activity by which the methyl group of AdoMet is transferred to GTP, leading to the formation of m(7)GTP, and the m(7)GMP moiety is next transferred to the 5' end of ppRNA via a covalent enzyme-m(7)GMP intermediate. The function of the conserved H68 of the BaMV capping enzyme in the intermediate formation was analyzed by mutagenesis in this study. The nature of the bond linking the enzyme and m(7)GMP was changed in the H68C mutant protein, strongly suggesting that H68 covalently binds to m(7)GMP in the intermediate. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2326 / 2331
页数:6
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