Document Detail


Yersinia enterocolitica type III secretion: mutational analysis of the yopQ secretion signal.
MedLine Citation:
PMID:  12029049     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Pathogenic Yersinia spp. secrete Yop proteins via the type III pathway. yopQ codons 1 to 15 were identified as a signal necessary and sufficient for the secretion of a fused reporter protein. Frameshift mutations that alter codons 2 to 15 with little alteration of yopQ mRNA sequence do not abolish type III transport, suggesting a model in which yopQ mRNA may provide a signal for secretion (D. M. Anderson and O. Schneewind, Mol. Microbiol. 31:1139-1148, 2001). In a recent study, the yopE signal was truncated to codons 1 to 12. All frameshift mutations introduced within the first 12 codons of yopE abolished secretion. Also, multiple synonymous mutations that changed the mRNA sequence of yopE codons 1 to 12 without altering the amino acid sequence did not affect secretion. These results favor a model whereby an N-terminal signal peptide initiates YopE into the type III pathway (S. A. Lloyd et al., Mol. Microbiol. 39:520-531, 2001). It is reported here that codons 1 to 10 of yopQ act as a minimal secretion signal. Further truncation of yopQ, either at codon 10 or at codon 2, abolished secretion. Replacement of yopQ AUG with either of two other start codons, UUG or GUG, did not affect secretion. However, replacement of AUG with CUG or AAA and initiating translation at the fusion site with npt did not permit Npt secretion, suggesting that the translation of yopQ codons 1 to 15 is a prerequisite for secretion. Frameshift mutations of yopQ codons 1 to 10, 1 to 11, and 1 to 12 abolished secretion signaling, whereas frameshift mutations of yopQ codons 1 to 13, 1 to 14, and 1 to 15 did not. Codon changes at yopQ positions 2 and 10 affected secretion signaling when placed within the first 10 codons but had no effect when positioned in the larger fusion of yopQ codons 1 to 15. An mRNA mutant of yopQ codons 1 to 10, generated by a combination of nine synonymous mutations, was defective in secretion signaling, suggesting that the YopQ secretion signal is not proteinaceous. A model is discussed whereby the initiation of YopQ polypeptide into the type III pathway is controlled by properties of yopQ mRNA.
Authors:
Kumaran S Ramamurthi; Olaf Schneewind
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of bacteriology     Volume:  184     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2002 Jun 
Date Detail:
Created Date:  2002-05-24     Completed Date:  2002-06-27     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3321-8     Citation Subset:  IM    
Affiliation:
Committee on Microbiology, University of Chicago, Chicago, Illinois 60637, USA.
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MeSH Terms
Descriptor/Qualifier:
3' Untranslated Regions
Bacterial Outer Membrane Proteins / genetics,  metabolism*
Base Sequence
Codon
DNA Mutational Analysis*
Frameshift Mutation
Gene Expression Regulation, Bacterial*
Molecular Sequence Data
Protein Biosynthesis
RNA, Messenger / genetics*
Signal Transduction*
Yersinia enterocolitica / genetics*,  metabolism
Grant Support
ID/Acronym/Agency:
AI42797/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/3' Untranslated Regions; 0/Bacterial Outer Membrane Proteins; 0/Codon; 0/RNA, Messenger; 131383-92-1/YopQ protein, Yersinia enterocolitica
Comments/Corrections

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