PMID:2186030
| Citation |
Gottesman, S, Clark, WP and Maurizi, MR (1990) The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. J. Biol. Chem. 265:7886-93 |
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| Abstract |
The clpA gene, which codes for the ATP-binding subunit of the ATP-dependent Clp protease of Escherichia coli, has been sequenced. The coding region contains a single open reading frame for a protein of 758 amino acids; within the amino acid sequence are two consensus sequences for ATP-binding sites. The sequence of ClpA does not resemble that of other previously described ATPases or Lon, the other sequenced ATP-dependent protease of E. coli, except in the ATP-binding site consensus region. The clpA gene is expressed as a monocistronic message. Primer extension experiments define a major start point of transcription at -183 relative to the start of translation. A rho-independent terminator is located 23 bases beyond the end of the coding region. The ClpA protein is degraded in vivo in a Clp-dependent fashion (t1/2 approximately 60 min). A fusion protein containing the first 40 amino acids of ClpA fused in frame to beta-galactosidase is degraded very rapidly in a clpA+ host (t1/2 approximately 3 min) but not in a clpA- host. This fusion protein is the first Clp-specific substrate described. |
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| Keywords |
ATP-Dependent Proteases; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Base Sequence; Binding Sites; Drug Stability; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression; Heat-Shock Proteins; Molecular Sequence Data; Molecular Weight; Protease La; Protein Conformation; Recombinant Fusion Proteins/metabolism; Restriction Mapping; Sequence Homology, Nucleic Acid; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism; Substrate Specificity; Transcription, Genetic |
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