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Volume 156, Issue 10

Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Free

Abstract

The phage-shock-protein (Psp) response maintains the proton-motive force (pmf) under extracytoplasmic stress conditions that impair the inner membrane (IM) in bacterial cells. In transcription of the and genes requires activation of -RNA polymerase by the enhancer-binding protein PspF. A regulatory network comprising PspF–A–C–B–ArcB controls expression. One key regulatory point is the negative control of PspF imposed by its binding to PspA. It has been proposed that under stress conditions, the IM-bound sensors PspB and PspC receive and transduce the signal(s) to PspA via protein–protein interactions, resulting in the release of the PspA–PspF inhibitory complex and the consequent induction of . In this work we demonstrate that PspB self-associates and interacts with PspC via putative IM regions. We present evidence suggesting that PspC has two topologies and that conserved residue G48 and the putative leucine zipper motif are determinants required for PspA interaction and signal transduction upon stress. We also establish that PspC directly interacts with the effector PspG, and show that PspG self-associates. These results are discussed in the context of formation and function of the Psp regulatory complex.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): Ara, l-arabinose , BACTH, bacterial two-hybrid , IM, inner membrane , LeuZ, leucine zipper motif , LeuZm, leucine zipper mutant , MU, Miller units , pIV, protein IV , pmf, proton-motive force , Psp, phage-shock protein , Sol, soluble fraction , TM, transmembrane , β-Gal, β-galactosidase and Δψ, electron potential
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2010-10-01
2024-04-23
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Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli
Microbiology 156, 2920 (2010); https://doi.org/10.1099/mic.0.040055-0
/content/journal/micro/10.1099/mic.0.040055-0
/content/journal/micro/10.1099/mic.0.040055-0
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