Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin

被引：178

作者：

Kamada, K

Hanaoka, F

机构：

[1] RIKEN, Discovery Res Inst, Cellular Physiol Lab, Wako, Saitama 3510198, Japan

[2] Osaka Univ, Grad Sch Frontier Biosci, Suita, Osaka 5650871, Japan

来源：

MOLECULAR CELL | 2005年 / 19卷 / 04期

基金：

日本科学技术振兴机构;

关键词：

D O I：

10.1016/j.molcel.2005.07.004

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 eubacterial chromosome encodes various addiction modules that control global levels of translation through RNA degradation. Crystal structures of the Escherichia coli YefM(2) (antitoxin)-YoeB (toxin) complex and the free YoeB toxin have been determined. The structure of the heterotrimeric complex reveals an asymmetric disorder-to-order recognition strategy, in which one C terminus of the YefM homodimer exclusively interacts with an atypical microbial ribonuclease (RNase) fold of YoeB. Comparison with the YefM-free YoeB structure indicates a conformational rearrangement of the RNase catalytic site of YoeB, induced by interaction with YefM. Complementary biochemical experiments demonstrate that the YoeB toxin has an in vitro RNase activity that preferentially cleaves at the 3' end of purine ribonucleotides.

引用

页码：497 / 509

页数：13

共 41 条

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