This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ramamurthi, K. S.
Right arrow Articles by Schneewind, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ramamurthi, K. S.
Right arrow Articles by Schneewind, O.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2005, p. 707-715, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.707-715.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Synonymous Mutation in Yersinia enterocolitica yopE Affects the Function of the YopE Type III Secretion Signal

Kumaran S. Ramamurthi{dagger} and Olaf Schneewind*

Department of Microbiology, University of Chicago, Chicago, Illinois

Received 22 July 2004/ Accepted 17 September 2004

Yersinia spp. inject virulence proteins called Yops into the cytosol of target eukaryotic cells in an effort to evade phagocytic killing via a dedicated protein-sorting pathway termed type III secretion. Previous studies have proposed that, unlike other protein translocation mechanisms, Yops are not recognized as substrates for secretion via a solely proteinaceous signal. Rather, at least some of this information may be encoded within yop mRNA. Herein, we report that the first seven codons of yopE, when fused to the reporter protein neomycin phosphotransferase (Npt), are sufficient for the secretion of YopE1-7-Npt when type III secretion is induced in vitro. Systematic mutagenesis of yopE codons 1 to 7 reveals that, like yopQ, codons 2, 3, 5, and 7 are sensitive to mutagenesis, thereby defining the first empirical similarity between the secretion signals of two type III secreted substrates. Like that of yopQ, the secretion signal of yopE exhibits a bipartite nature. This is manifested by the ability of codons 8 to 15 to suppress point mutations in the minimal secretion signal that change the amino acid specificities of particular codons or that induce alterations in the reading frame. Further, we have identified a single nucleotide position in codon 3 that, when mutated, conserves the predicted amino acid sequence of the YopE1-7-Npt but abrogates secretion of the reporter protein. When introduced into the context of the full-length yopE gene, the single-nucleotide mutation reduces the type III injection of YopE into HeLa cells, even though the predicted amino acid sequence remains the same. Thus, yopE mRNA appears to encode a property that mediates the type III injection of YopE.

* Corresponding author. Mailing address: Department of Microbiology, University of Chicago, 920 East 58th St., Chicago, IL 60637. Phone: (773) 834-9060. Fax: (773) 834-8150. E-mail: oschnee{at}bsd.uchicago.edu.

{dagger} Present address: Department of Molecular and Cellular Biology, The Biological Laboratories, Harvard University, Cambridge, MA 02138.

Journal of Bacteriology, January 2005, p. 707-715, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.707-715.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Riordan, K. E., Sorg, J. A., Berube, B. J., Schneewind, O. (2008). Impassable YscP Substrates and Their Impact on the Yersinia enterocolitica Type III Secretion Pathway. J. Bacteriol. 190: 6204-6216 [Abstract] [Full Text]  
  • Rodgers, L., Gamez, A., Riek, R., Ghosh, P. (2008). The Type III Secretion Chaperone SycE Promotes a Localized Disorder-to-Order Transition in the Natively Unfolded Effector YopE. J. Biol. Chem. 283: 20857-20863 [Abstract] [Full Text]  
  • Kim, H. G., Kim, B. H., Kim, J. S., Eom, J. S., Bang, I.-S., Bang, S. H., Lee, I. S., Park, Y. K. (2008). N-terminal residues of SipB are required for its surface localization on Salmonella enterica serovar Typhimurium. Microbiology 154: 207-216 [Abstract] [Full Text]  
  • Kim, B. H., Kim, H. G., Kim, J. S., Jang, J. I., Park, Y. K. (2007). Analysis of functional domains present in the N-terminus of the SipB protein. Microbiology 153: 2998-3008 [Abstract] [Full Text]  
  • Blaylock, B., Riordan, K. E., Missiakas, D. M., Schneewind, O. (2006). Characterization of the Yersinia enterocolitica Type III Secretion ATPase YscN and Its Regulator, YscL.. J. Bacteriol. 188: 3525-3534 [Abstract] [Full Text]  
  • Sorg, J. A., Miller, N. C., Marketon, M. M., Schneewind, O. (2005). Rejection of Impassable Substrates by Yersinia Type III Secretion Machines. J. Bacteriol. 187: 7090-7102 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»