Activity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners

18Citations
Citations of this article
30Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Background: Regulation of the bacterial phage shock protein (Psp) stress response is poorly understood. Results: The C-terminal domain of PspC (PspCCT) can interact with PspA or PspB. Conclusion: Induction of psp gene expression involves a PspCCT binding partner switch from PspB to PspA. Significance: Understanding the activation mechanism is critical because this system is essential for virulence in Yersinia enterocolitica and Salmonella enterica.

Cite

CITATION STYLE

APA

Flores-Kim, J., & Darwin, A. J. (2015). Activity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners. Journal of Biological Chemistry, 290(18), 11417–11430. https://doi.org/10.1074/jbc.M114.614107

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free