Self-assembly of Escherichia coli phage shock protein A
Self-assembly of Escherichia coli phage shock protein A
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.
353-359
Male, Abigail
cad6c2bc-04df-4078-b5d2-9f3c808e6152
Tavassoli, Ali
d561cf8f-2669-46b5-b6e1-2016c85d63b2
May 2014
Male, Abigail
cad6c2bc-04df-4078-b5d2-9f3c808e6152
Tavassoli, Ali
d561cf8f-2669-46b5-b6e1-2016c85d63b2
Male, Abigail and Tavassoli, Ali
(2014)
Self-assembly of Escherichia coli phage shock protein A.
Advances in Microbiology, 4 (7), .
(doi:10.4236/aim.2014.47042).
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.
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Published date: May 2014
Organisations:
Organic Chemistry: SCF
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Local EPrints ID: 371643
URI: http://eprints.soton.ac.uk/id/eprint/371643
ISSN: 2165-3402
PURE UUID: 128f2c25-f892-4165-a172-c76c32e429c3
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Date deposited: 11 Nov 2014 11:24
Last modified: 15 Mar 2024 03:26
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Author:
Abigail Male
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