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Title 

Structural basis of mRNA recognition and cleavage by toxin MazF and its regulation by antitoxin MazE in Bacillus subtilis

 

Bacillus subtilis에서 MazF toxin의 mRNA 인식 및 절단 그리고 MazE antitoxin의 인식에 대한 단백질 구조분석

Authors 

D K SimanshuY YamaguchiJung Ho ParkM InouyeD J Patel

Publisher 

Elsevier (Cell Press)

Issue Date 

2013

Citation 

Molecular Cell, vol. 52, no. 3, pp. 447-458

Abstract 

MazF is an mRNA interferase, which, upon activation during stress conditions, cleaves mRNAs in a sequence-specific manner, resulting in cellular growth arrest. During normal growth conditions, the MazF toxin is inactivated through binding to its cognate antitoxin, MazE. How MazF specifically recognizes its mRNA target and carries out cleavage and how the formation of the MazE-MazF complex inactivates MazF remain unclear. We present crystal structures of MazF in complex with mRNA substrate and antitoxin MazE in Bacillus subtilis. The structure of MazF in complex with uncleavable UUdUACAUAA RNA substrate defines the molecular basis underlying the sequence-specific recognition of UACAU and the role of residues involved in the cleavage through site-specific mutational studies. The structure of the heterohexameric (MazF)2-(MazE)2-(MazF)2 complex in Bacillus subtilis, supplemented by mutational data, demonstrates that the positioning of the C-terminal helical segment of MazE within the RNA-binding channel of the MazF dimer prevents mRNA binding and cleavage by MazF.

ISSN 

1097-2765

Link 

http://dx.doi.org/10.1016/j.molcel.2013.09.006

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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