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Chapter 6 : Role of Proteolysis and Chaperones in Stress Response and Regulation

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Role of Proteolysis and Chaperones in Stress Response and Regulation, Page 1 of 2

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Abstract:

This chapter presents selected examples of general and regulatory proteolysis, which are important for bacterial stress response. Chaperones and proteases systems are intricately connected and embedded in the regulation of stress response, in sensing stress via unfolded protein species, and in controlling the activity of the respective transcription factors. The major proteins involved in general degradation are Hsp100/Clp proteins or AAA+ proteases. In the heat shock control a repressor is kept active, whereas in the system an activator is kept inactive by molecular chaperones, both resulting in the inhibition of stress response under normal growth conditions. Controlled proteolysis of regulatory proteins by the Hsp100/Clp AAA+ protease systems has also been adapted in evolution for regulation of developmental processes that can, but must not necessarily, be considered as stress response pathways. The periplasma is a special compartment in gram-negative bacteria, and the integrity and functioning of proteins localized or passing through that compartment are very important for the cell. Therefore, a protein quality control system and a stress response system with specialized chaperones and proteases, such as DegP, for this compartment is present in . The trans-membrane signaling RIP signaling pathway can also be used to sense and regulate stress response as introduced for the control of the activity of the ECF σ factors σ of and σ of .

Citation: Turgay K. 2011. Role of Proteolysis and Chaperones in Stress Response and Regulation, p 75-90. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch6

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Figures

Image of Figure 1.
Figure 1.

Hsp100/Clp and AAA+ protease complexes. First row: a schematic diagram of the different bacterial Hsp100/Clp and AAA+ protease complexes. Second row: adaptor and associated proteins interacting with these protein complexes. Third row: protein domains and subdomains of these complexes.

Citation: Turgay K. 2011. Role of Proteolysis and Chaperones in Stress Response and Regulation, p 75-90. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch6
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Image of Figure 2.
Figure 2.

(a) General mechanism of protein degradation by Hsp100/Clp proteins. (b) Adaptor protein-mediated activation of ClpCP.

Citation: Turgay K. 2011. Role of Proteolysis and Chaperones in Stress Response and Regulation, p 75-90. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch6
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Image of Figure 3.
Figure 3.

Regulatory proteolysis. (a) Class III heat shock response in . (b) Regulation of competence development in . (c) Control of RpoS stability in .

Citation: Turgay K. 2011. Role of Proteolysis and Chaperones in Stress Response and Regulation, p 75-90. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch6
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Image of Figure 4.
Figure 4.

Schematic outline of regulated intramembrane proteolysis in bacteria. See text for details.

Citation: Turgay K. 2011. Role of Proteolysis and Chaperones in Stress Response and Regulation, p 75-90. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch6
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