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J Biol Chem. 1990 May 15;265(14):7886-93.

The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate.

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  • 1Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.


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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