Document Detail


YscU recognizes translocators as export substrates of the Yersinia injectisome.
MedLine Citation:
PMID:  17510628     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
YscU is an essential component of the export apparatus of the Yersinia injectisome. It consists of an N-terminal transmembrane domain and a long cytoplasmic C-terminal domain, which undergoes auto-cleavage at a NPTH site. Substitutions N263A and P264A prevented cleavage of YscU and abolished export of LcrV, YopB and YopD but not of Yop effectors. As a consequence, yscU(N263A) mutant bacteria made needles without the LcrV tip complex and they could not form translocation pores. The graft of the export signal of the effector YopE, at the N-terminus of LcrV, restored LcrV export and assembly of the tip complex. Thus, YscU cleavage is required to acquire the conformation allowing recognition of translocators, which represent an individual category of substrates in the hierarchy of export. In addition, yscU(N263A) mutant bacteria exported reduced amounts of the YscP ruler and made longer needles. Increasing YscP export resulted in needles with normal size, depending on the length of the ruler. Hence, the effect of the yscU(N263A) mutation on needle length was the consequence of a reduced YscP export.
Authors:
Isabel Sorg; Stefanie Wagner; Marlise Amstutz; Shirley A Müller; Petr Broz; Yvonne Lussi; Andreas Engel; Guy R Cornelis
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-05-17
Journal Detail:
Title:  The EMBO journal     Volume:  26     ISSN:  0261-4189     ISO Abbreviation:  EMBO J.     Publication Date:  2007 Jun 
Date Detail:
Created Date:  2007-06-20     Completed Date:  2007-09-20     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  England    
Other Details:
Languages:  eng     Pagination:  3015-24     Citation Subset:  IM    
Affiliation:
Infection Biology, Biozentrum der Universität Basel, Klingelbergstrasse 50-70, CH 4056 Basel, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / genetics,  metabolism*
Microscopy, Electron, Transmission
Mutation
Protein Binding
Protein Transport
Yersinia / metabolism*,  ultrastructure
Chemical
Reg. No./Substance:
0/Bacterial Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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