Yamaguchi, S., Reid, D.A., Rothenberg, E. and Darwin, A.J. (2013) Changes in Psp Protein Binding Partners, Localization and Behaviour upon Activation of the Yersinia enterocolitica Phage Shock Protein Response. Molecular Microbiology, 87, 656-671.
http://dx.doi.org/10.1111/mmi.12122

has been cited by the following article:

• TITLE: Self-Assembly of Escherichia coli Phage Shock Protein A

  AUTHORS: Abigail L. Male, Petra C. F. Oyston, Ali Tavassoli

  KEYWORDS: Phage Shock Protein A, Stress Response, Membrane Stress, Super-Complex, Self-Assembly

  JOURNAL NAME: Advances in Microbiology, Vol.4 No.7, May 19, 2014

  ABSTRACT: The Phage shock protein (Psp) response is an extracytoplasmic stress response. The central component of this system is PspA, a protein that mediates the physiological response to membrane stress. PspA is also involved in regulating its own transcription and that of the psp operon, forming a positive feedback loop. PspA has been previously shown to oligomerise into higher-order species, including a 36-meric species with ring-like structure. In this study, we demonstrate that the ring-like PspA structures further self-assemble into rod-shaped complexes. These rod-like structures may play a scaffolding role in the maintenance of membrane integrity during phage shock protein response.