PMID:14536075
| Citation |
Wah, DA, Levchenko, I, Rieckhof, GE, Bolon, DN, Baker, TA and Sauer, RT (2003) Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Mol. Cell 12:355-63 |
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| Abstract |
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. |
| Links | |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphate/metabolism; Adhesins, Bacterial/chemistry; Adhesins, Bacterial/metabolism; Amino Acid Sequence; Bacterial Proteins/physiology; Binding Sites; Dimerization; Dose-Response Relationship, Drug; Endopeptidase Clp; Escherichia coli/metabolism; Escherichia coli Proteins; Green Fluorescent Proteins; Hydrolysis; Luminescent Proteins/metabolism; Models, Biological; Molecular Chaperones; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; RNA, Bacterial/metabolism; Sequence Homology, Amino Acid; Serine Endopeptidases/chemistry; Substrate Specificity |
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