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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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ATPases Associated with Diverse Cellular Activities
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphate / metabolism
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Adhesins, Bacterial / chemistry*
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Adhesins, Bacterial / metabolism
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Amino Acid Sequence
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Bacterial Proteins / physiology
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Binding Sites
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Dimerization
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Dose-Response Relationship, Drug
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Endopeptidase Clp
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Escherichia coli / metabolism
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Escherichia coli Proteins*
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Green Fluorescent Proteins
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Hydrolysis
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Luminescent Proteins / metabolism
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Models, Biological
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Molecular Chaperones
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Molecular Sequence Data
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Mutation
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Protein Binding
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Protein Structure, Tertiary
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RNA, Bacterial / metabolism
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Sequence Homology, Amino Acid
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Serine Endopeptidases / chemistry*
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Substrate Specificity
Substances
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Adhesins, Bacterial
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Bacterial Proteins
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Escherichia coli Proteins
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Luminescent Proteins
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Molecular Chaperones
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RNA, Bacterial
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tmRNA
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salivary agglutinin receptor, Streptocococcus
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Green Fluorescent Proteins
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Adenosine Triphosphate
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Serine Endopeptidases
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ClpXP protease, E coli
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Endopeptidase Clp
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Adenosine Triphosphatases
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ClpX protein, E coli
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ATPases Associated with Diverse Cellular Activities