Localization of general and regulatory proteolysis in Bacillus subtilis cells

Janine Kirstein, Henrik Strahl, Noël Molière, Leendert W. Hamoen, Kürşad Turgay

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Protein degradation mediated by ATP-dependent proteases, such as Hsp100/Clp and related AAA+ proteins, plays an important role in cellular protein homeostasis, protein quality control and the regulation of, e.g. heat shock adaptation and other cellular differentiation processes. ClpCP with its adaptor proteins and other related proteases, such as ClpXP or ClpEP of Bacillus subtilis, are involved in general and regulatory proteolysis. To determine if proteolysis occurs at specific locations in B. subtilis cells, we analysed the subcellular distribution of the Clp system together with adaptor and general and regulatory substrate proteins, under different environmental conditions. We can demonstrate that the ATPase and the proteolytic subunit of the Clp proteases, as well as the adaptor or substrate proteins, form visible foci, representing active protease clusters localized to the polar and to the mid-cell region. These clusters could represent a compartmentalized place for protein degradation positioned at the pole close to where most of the cellular protein biosynthesis and also protein quality control are taking place, thereby spatially separating protein synthesis and degradation.

Original languageEnglish
Pages (from-to)682-694
Number of pages13
JournalMolecular Microbiology
Volume70
Issue number3
DOIs
Publication statusPublished - Nov 2008
Externally publishedYes

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