HpaC Controls Substrate Specificity of the Xanthomonas Type III Secretion System

PLoS Pathogens

Ombeline Rossier¹  Ulla Bonas¹  Thomas Wolsch¹  Steve Schulz¹  Daniela Büttner¹  Christian Lorenz¹ 

[1] Institut für Biologie, Bereich Genetik, Martin-Luther-Universität Halle-Wittenberg, Halle (Saale), Germany

关键词: Protein secretion;    Glutathione chromatography;    Xanthomonas campestris;    Secretion;    Protein domains;    Pili;    fimbriae;    Immunoblotting;    Plant bacterial pathogens;   

DOI  :  10.1371/journal.ppat.1000094

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

The Gram-negative bacterial plant pathogen Xanthomonas campestris pv. vesicatoria employs a type III secretion (T3S) system to inject bacterial effector proteins into the host cell cytoplasm. One essential pathogenicity factor is HrpB2, which is secreted by the T3S system. We show that secretion of HrpB2 is suppressed by HpaC, which was previously identified as a T3S control protein. Since HpaC promotes secretion of translocon and effector proteins but inhibits secretion of HrpB2, HpaC presumably acts as a T3S substrate specificity switch protein. Protein–protein interaction studies revealed that HpaC interacts with HrpB2 and the C-terminal domain of HrcU, a conserved inner membrane component of the T3S system. However, no interaction was observed between HpaC and the full-length HrcU protein. Analysis of HpaC deletion derivatives revealed that the binding site for the C-terminal domain of HrcU is essential for HpaC function. This suggests that HpaC binding to the HrcU C terminus is key for the control of T3S. The C terminus of HrcU also provides a binding site for HrpB2; however, no interaction was observed with other T3S substrates including pilus, translocon and effector proteins. This is in contrast to HrcU homologs from animal pathogenic bacteria suggesting evolution of distinct mechanisms in plant and animal pathogenic bacteria for T3S substrate recognition.

【 授权许可】

CC BY