Work

Interaction of intramembrane metalloprotease SpoIVFB with substrate Pro-σ K

Year: 2017

Type: article

Abstract: Significance Most proteases catalyze peptide bond hydrolysis of substrate proteins in aqueous environments. Intramembrane proteases (IPs) are unusual, cleaving substrates in hydrophobic cellular membranes. IPs regulate many processes that impact health, but potential benefits of manipulating IP activities remain elusive due to insufficient knowledge about how IPs interact with substrates. We report experimental and modeling results that illuminate how intramembrane metalloprotease SpoIVFB interacts with its substrate Pro-σ K . A 26-residue linker between two domains of SpoIVFB is crucial, perhaps allowing an ATP-induced conformational change to position Pro-σ K for cleavage. SpoIVFB and Pro-σ K are broadly conserved in endospore-forming bacteria. Endospores are highly resistant cells that promote persistence of some important human pathogens. The work may lead to new strategies to control endospore formation.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1711467114

Authors: Sabyasachi Halder, Daniel Parrell, Douglas Whitten, Michael Feig, Lee Kroos

Institution: Michigan State University

Language: English

Topic: Bacterial Genetics and Biotechnology

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: AgBioResearch, Michigan State University, National Institute of General Medical Sciences

Awards: G3079679661, G3874334470, G5133205949