Lookup NU author(s): Dr Henrik Strahl von Schulten,
Dr Leendert Hamoen
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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.
Author(s): Kirstein J, Strahl H, Moliere N, Hamoen LW, Turgay K
Publication type: Article
Journal: Molecular Microbiology
ISSN (print): 0950-382X
ISSN (electronic): 1365-2958
Publisher: Wiley-Blackwell Publishing Ltd.
Notes: Kirstein, Janine
Hamoen, Leendert W
Biotechnology and Biological Sciences Research Council/United Kingdom
Wellcome Trust/United Kingdom
Research Support, Non-U.S. Gov't
Mol Microbiol. 2008 Nov;70(3):682-94. Epub 2008 Sep 10.
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