Structural Basis of mRNA Recognition and Cleavage by Toxin MazF and Its Regulation by Antitoxin MazE in Bacillus subtilis Journal Article

   

Authors:	Simanshu, D. K.; Yamaguchi, Y.; Park, J. H.; Inouye, M.; Patel, D. J.
Article Title:	Structural Basis of mRNA Recognition and Cleavage by Toxin MazF and Its Regulation by Antitoxin MazE in Bacillus subtilis
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. © 2013 Elsevier Inc.
Journal Title:	Molecular Cell
Volume:	52
Issue:	3
ISSN:	1097-2765
Publisher:	Cell Press
Date Published:	2013-11-07
Start Page:	447
End Page:	458
Language:	English
DOI:	10.1016/j.molcel.2013.09.006
PROVIDER:	scopus
PUBMED:	24120662
PMCID:	PMC4691852
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-84887166572&partnerID=40&md5=55358566e06417cab8464b1591133577
Notes:	- "Export Date: 2 December 2013" - "CODEN: MOCEF" - "Source: Scopus"

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