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Papers In Press, published online ahead of print January 2, 2002
J. Biol. Chem, 10.1074/jbc.M111278200
Submitted on November 27, 2001
Revised on December 21, 2001
Accepted on January 2, 2002
Cell Biology, Institute for Molecular and Cellular Biology, Osaka University, Suita, Osaka 565-0871
Corresponding Author: fhanaoka{at}imcb.osaka-u.ac.jp
Escherichia coli DNA gyrase is comprised of two subunits, GyrA and GyrB. Previous studies have shown that GyrI, a regulatory factor of DNA gyrase activity, inhibits the supercoiling activity of DNA gyrase, and that both overexpression and antisense expression of the gyrI gene suppress cell proliferation. Here we have analyzed the interaction of GyrI with DNA gyrase using two approaches. First, immunoprecipitation experiments revealed that GyrI interacts preferentially with the holoenzyme in an ATP-independent manner, although a weak interaction was also detected between GyrI and the individual GyrA and GyrB subunits. Second, surface plasmon resonance (SPR) experiments indicated that GyrI binds to the gyrase holoenzyme with higher affinity than to either the GyrA or GyrB subunits alone. Unlike quinolone antibiotics, GyrI was not effective in stabilizing the cleavable complex consisting of gyrase and DNA. Further, we identified an 8-residue synthetic peptide, corresponding to amino acids 89-ITGGQYAV-96 of GyrI, that inhibits gyrase activity in an in vitro supercoiling assay. SPR analysis of the ITGGQYAV-containing peptide-gyrase interaction indicated a high association constant for this interaction. These results suggest that amino acids 89-96 of GyrI is essential for its interaction with, and inhibition of, DNA gyrase.
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