Identification of inducers of the Yersinia enterocolitica phage shock protein system and comparison to the regulation of the RpoE and Cpx extracytoplasmic stress responses.
Known inducers of the phage shock protein (Psp) system suggest that it is an extracytoplasmic stress response, as are the well-studied RpoE and Cpx systems. However, a random approach to identify conditions and proteins that induce the Psp system has not been attempted. It is also unknown whether the proteins or mutations that induce Psp are specific or if they also activate the RpoE and Cpx systems. This study addressed these issues for the Yersinia enterocolitica Psp system. Random transposon mutagenesis identified null mutations and overexpression mutations that increase Phi(pspA-lacZ) operon fusion expression. The results suggest that Psp may respond exclusively to extracytoplasmic stress. Null mutations affected glucosamine-6-phosphate synthetase (glmS), which plays a role in cell envelope biosynthesis, and the F0F1 ATPase (atp operon). The screen also revealed that in addition to several secretins, the overexpression of three novel putative inner membrane proteins (IMPs) induced the Psp response. We also compared induction of the Y. enterocolitica Psp, RpoE, and Cpx responses. Overexpression of secretins or the three IMPs or the presence of an atpB null mutation only induced the Psp response. Similarly, known inducers of the RpoE and Cpx responses did not significantly induce the Psp response. Only the glmS null mutation induced all three responses. Therefore, Psp is induced distinctly from the RpoE and Cpx systems. The specific IMP inducers may be valuable tools to probe specific signal transduction events of the Psp response in future studies.
Maxson
Michelle E
ME
Department of Microbiology, New York University School of Medicine, New York, New York 10016, USA.
Darwin
Andrew J
AJ
D001426:Bacterial Proteins / Q000096:biosynthesis*; D001483:Base Sequence; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006863:Hydrogen-Ion Concentration; D008565:Membrane Proteins / Q000502:physiology*; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000502:physiology; D012808:Sigma Factor / Q000502:physiology*; D014157:Transcription Factors / Q000502:physiology*; D015008:Yersinia enterocolitica / Q000235:genetics / Q000254:growth & development / Q000502:physiology*
D001426:Bacterial Proteins; C110674:CpxP protein, bacteria; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C069816:phage shock protein, Bacteria; C063202:sporulation-specific sigma factors; D006180:Proton-Translocating ATPases