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J Biol Chem, Vol. 274, Issue 37, 26225-26232, September 10, 1999
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From the Escherichia coli FtsH is an
ATP-dependent protease that belongs to the AAA protein
family. The second region of homology (SRH) is a highly conserved motif
among AAA family members and distinguishes these proteins in part from
the wider family of Walker-type ATPases. Despite its conservation
across the AAA family of proteins, very little is known concerning the
function of the SRH. To address this question, we introduced point
mutations systematically into the SRH of FtsH and studied the
activities of the mutant proteins. Highly conserved amino acid residues
within the SRH were found to be critical for the function of FtsH, with
mutations at these positions leading to decreased or abolished ATPase
activity. The effects of the mutations on the protease activity of FtsH
correlated strikingly with their effects on the ATPase activity. The
ATPase-deficient SRH mutants underwent an ATP-induced conformational
change similar to wild type FtsH, suggesting an important role for the
SRH in ATP hydrolysis but not ATP binding. Analysis of the data in the light of the crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein suggests a
plausible mechanism of ATP hydrolysis by the AAA ATPases, which invokes an intermolecular catalytic role for the SRH.
Department of Molecular Cell Biology,
Institute of Molecular Embryology and Genetics, Kumamoto University
School of Medicine, Kumamoto 862-0976, Japan and the
§ Department of Chemistry, University of York,
York YO1 5DD, United Kingdom
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