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Article

Membrane Chaperoning of a Thylakoid Protease Whose Structural Stability Is Modified by the Protonmotive Force.

The Plant cell - 1 May 2020

McKinnon Lucas J, Fukushima Jeremy, Endow Joshua K, Inoue Kentaro, Theg Steven M

Abstract excerpt

Protein folding is a complex cellular process often assisted by chaperones, but it can also be facilitated by interactions with lipids. Disulfide bond formation is a common mechanism to stabilize a protein. This can help maintain functionality amid changes in the biochemical milieu, including those relating to energy-transducing membranes. Plastidic Type I Signal Peptidase 1 (Plsp1) is an integral thylakoid...

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Identifiers

PMID: 32169961
DOI: 10.1105/tpc.19.00797
PMCID: PMC7203927

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