Peptidic small molecule activators of the stress sensor DegS

Hauske, Patrick, Mamant, Nicolette, Hasenbein, Sonja, Nickel, Sabrina, Ottmann, Christian, Clausen, Tim, Ehrmann, Michael ORCID: https://orcid.org/0000-0002-1927-260X and Kaiser, Markus 2009. Peptidic small molecule activators of the stress sensor DegS. Molecular Biosystems 5 (9) , pp. 980-985. 10.1039/b902089f

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Abstract

Bacterial DegS is a regulatory protease that acts as a molecular stress sensor and initiates a periplasmic stress response pathway. Upon binding of misfolded proteins to its PDZ domain, the protease domain of DegS is allosterically activated, thereby initiating a signal cascade that results in the elevated expression of protein quality control factors. Although the structural basis of this activation mode has been elucidated previously, it is not yet fully understood if binding to the PDZ domain is sufficient for protease domain activation or if secondary interactions with the protease domain are required. Here, we demonstrate that tripeptidic small molecule activators which only bind to the PDZ domain are sufficient to trigger DegS activation. Furthermore, we show that the hydrophobicity of the peptidic small molecule activators is a critical determinant for efficient activation.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Subjects:	Q Science > QH Natural history > QH301 Biology
Publisher:	Royal Society of Chemistry
ISSN:	1742-206X
Last Modified:	25 Oct 2022 09:14
URI:	https://orca.cardiff.ac.uk/id/eprint/57789

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