Journal
MOLECULAR CELL
Volume 12, Issue 2, Pages 355-363Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(03)00272-7
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Funding
- NIAID NIH HHS [AI-16892] Funding Source: Medline
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SspB dimers bind proteins bearing the ssrA-degradation tag and stimulate their degradation by the ClpXP protease. Here, E. coli SspB is shown to contain a dimeric substrate binding domain of 110-120 N-terminal residues, which binds ssrA-tagged substrates but does not stimulate their degradation. The C-terminal 40-50 residues of SspB are unstructured but are required for SspB to form substrate-delivery complexes with ClpXP. A synthetic peptide containing the 10 C-terminal residues of SspB binds ClpX, stimulates its ATPase activity, and prevents SspB-mediated delivery of GFP-ssrA for ClpXP degradation. This tripartite structure-an ssrA-tag binding and dimerization domain, a flexible linker, and a short peptide module that docks with ClpX-allows SspB to deliver tagged substrates to ClpXP without interfering with their denaturation or degradation.
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