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Journal of Bacteriology, July 2004, p. 4110-4123, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4110-4123.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The YopD Translocator of Yersinia pseudotuberculosis Is a Multifunctional Protein Comprised of Discrete Domains

Jan Olsson,1,{dagger} Petra J. Edqvist,1,{dagger} Jeanette E. Bröms,1,2,{dagger} Åke Forsberg,1,2 Hans Wolf-Watz,1 and Matthew S. Francis1*

Department of Molecular Biology, Umeå University, SE-901 87 Umeå,1 Department of Medical Countermeasures, Swedish Defence Research Agency, Division of NBC-Defence, SE-901 82 Umeå, Sweden2

Received 19 January 2004/ Accepted 25 March 2004

To establish an infection, Yersinia pseudotuberculosis utilizes a plasmid-encoded type III translocon to microinject several anti-host Yop effectors into the cytosol of target eukaryotic cells. YopD has been implicated in several key steps during Yop effector translocation, including maintenance of yop regulatory control and pore formation in the target cell membrane through which effectors traverse. These functions are mediated, in part, by an interaction with the cognate chaperone, LcrH. To gain insight into the complex molecular mechanisms of YopD function, we performed a systematic mutagenesis study to search for discrete functional domains. We highlighted amino acids beyond the first three N-terminal residues that are dispensable for YopD secretion and confirmed that an interaction between YopD and LcrH is essential for maintenance of yop regulatory control. In addition, discrete domains within YopD that are essential for both pore formation and translocation of Yop effectors were identified. Significantly, other domains were found to be important for effector microinjection but not for pore formation. Therefore, YopD is clearly essential for several discrete steps during efficient Yop effector translocation. Recognition of this modular YopD domain structure provides important insights into the function of YopD.

* Corresponding author. Mailing address: Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden. Phone: 46-(0)90-7852536. Fax: 46-(0)90-771420. E-mail: matthew.francis{at}molbiol.umu.se.

{dagger} J.O., P.J.E., and J.E.B. contributed equally to this work.

Journal of Bacteriology, July 2004, p. 4110-4123, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4110-4123.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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