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J. Biol. Chem., Vol. 265, Issue 14, 7886-7893, May, 1990
S Gottesman, WP Clark and MR Maurizi
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.
The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
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