Satre M, Bof M, Vignais PV.Interaction of Escherichia coli
adenosine triphosphatase with aurovertin and citreoviridin:
inhibition and fluorescence studies.
J Bacteriol. 1980 Jun;142(3):768-76.
Aurovertins B and D inhibited the adenosine triphosphatase
(ATPase) activity of soluble Escherichia coli coupling factor
ATPase (BF1) isolated from wile-type E. coli K-12. Half
inhibition was obtained with 2 microns aurovertin B and 0.9
microns aurovertin D. Aurovertins B and D had no inhibitory
effect on BF1 isolated from the aurovertin-resistant E. coli
mutant MA12. Acetylation or saponification of aurovertin D
yielded a derivative which was devoid of inhibitory effect on
BF1. Citreoviridin also inhibited wild-type BF1 but with much
less efficiency (half inhibition at 60 microns) than aurovertin.
Citreoviridin had no effect on the aurovertin-resistant BF1. The
fluorescence intensity of aurovertins B and D was markedly
enhanced upon addition to purified BF1. There was no enhancement
of fluorescence when the aurovertins were added to BF1 isolated
from the aurovertin-resistant mutant. The fluorescence of the
aurovertin-BF1 complex was enhanced by adenosine 5'-diphosphate
and by low concentrations of adenosine 5'-triphosphate. The
adenosine 5'-diphosphate-enhanced fluorescence of the
aurovertin-BF1 complex was quenched by high concentrations of
adenosine 5'-triphosphate or by MG2+. Aurovertin bound
selectively to the beta subunit of BF1 isolated from wile-type
cells. By complementation assays in vitro, using a reconstituted
system made of subunits isolated from wild-type and aurovertin-resistant
BF1, it was shown that the altered peptide in aurovertin-resistant
BF1 was the beta subunit.
PMID: 6445896 |
