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.
Cite
CITATION STYLE
Male, A. L., Oyston, P. C. F., & Tavassoli, A. (2014). Self-Assembly of Escherichia coli Phage Shock Protein A. Advances in Microbiology, 04(07), 353–359. https://doi.org/10.4236/aim.2014.47042
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