PMID:11344323
| Citation |
Lo, JH, Baker, TA and Sauer, RT (2001) Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase. Protein Sci. 10:551-9 |
|---|---|
| Abstract |
The ClpA, ClpB, and ClpC subfamilies of the Clp/HSP100 ATPases contain a conserved N-terminal region of approximately 150 residues that consists of two approximate sequence repeats. This sequence from the Escherichia coli ClpA enzyme is shown to encode an independent structural domain (the R domain) that is monomeric and approximately 40% alpha-helical. A ClpA fragment lacking the R domain showed ATP-dependent oligomerization, protein-stimulated ATPase activity, and the ability to complex with the ClpP peptidase and mediate degradation of peptide and protein substrates, including casein and ssrA-tagged proteins. Compared with the activities of the wild-type ClpA, however, those of the ClpA fragment missing the R domain were reduced. These results indicate that the R domain is not required for the basic recognition, unfolding, and translocation functions that allow ClpA-ClpP to degrade some protein substrates, but they suggest that it may play a role in modulating these activities. |
| Links |
PubMed PMC2374137 Online version:10.1110/ps.41401 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Biophysical Phenomena; Biophysics; Endopeptidase Clp; Enzyme Activation; Escherichia coli/classification; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Hydrolysis; Mutagenesis/genetics; Protein Structure, Tertiary; Sequence Deletion/genetics; Sequence Homology; Serine Endopeptidases/chemistry; Serine Endopeptidases/metabolism; Terminal Repeat Sequences |
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