Abstract
ClpX, a molecular chaperone and the regulatory subunit of the ClpXP protease, is shown to contain tandem modular domains that bind to the C-terminal sequences of target proteins in a manner that parallels functional specificity. Nuclear magnetic resonance studies show that these C-terminal sequences are displayed as disordered peptides on the surface of otherwise folded proteins. The ClpX substrate-binding domains are homologous to sequences in other Clp/Hsp100 proteins and are related more distantly to PDZ domains, which also mediate C-terminal specific protein-protein interactions. Conservation of these binding domains indicates that the mode of substrate recognition characterized here for ClpX will be a conserved feature among Clp/Hsp100 family members and a distinguishing characteristic between this chaperone family and the Hsp70 chaperones.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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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 / metabolism*
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Amino Acid Sequence
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Binding Sites
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Endopeptidase Clp
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Escherichia coli
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Escherichia coli Proteins
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Heat-Shock Proteins / metabolism*
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Magnetic Resonance Spectroscopy
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Molecular Chaperones / metabolism*
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Molecular Sequence Data
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Protein Binding
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Protein Conformation
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Protein Folding
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Protozoan Proteins / metabolism*
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Serine Endopeptidases / metabolism*
Substances
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Escherichia coli Proteins
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Heat-Shock Proteins
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Molecular Chaperones
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Protozoan Proteins
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Serine Endopeptidases
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Endopeptidase Clp
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Adenosine Triphosphatases
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ClpB protein, Leishmania
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ClpX protein, E coli
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ATPases Associated with Diverse Cellular Activities
Associated data
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PDB/P03815
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PDB/P15716
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PDB/P23865
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PDB/P31007
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PDB/P31016
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PDB/P31539