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(Received for publication, July 29, 1996)
From the The product of the Escherichia coli
lon gene is the ATP-dependent Lon protease. Lon
contributes to the regulation of several important cellular functions,
including radiation resistance, cell division, filamentation, capsular
polysaccharide production, lysogeny of certain bacteriophages, and
proteolytic degradation of certain regulatory and abnormal proteins.
Lon homologues are also found in several widely divergent bacteria, as
well as in the mitochondria of yeast and humans. E. coli
Lon has long been known to bind to DNA, but this interaction has not
been further characterized and has generally been assumed to be
nonspecific. We now demonstrate that E. coli Lon can bind
to a TG-rich DNA promoter element in a sequence-specific manner. This
finding is based on the results of experiments employing SouthWestern
blotting, protein purification, "shift-shift" electrophoretic
mobility shift assays, electrophoretic mobility shift assays using
in vitro transcribed and translated Lon, and DNase
footprinting. Site-specific DNA binding is likely to be an additional
important biochemical characteristic of the multifaceted Lon
protease.
Volume 272, Number 1,
Issue of January 3, 1997
pp. 534-538
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
and
Department of Internal Medicine, Division of
Infectious Diseases, University of Michigan Medical Center, Ann
Arbor, Michigan 48109-0642 and the § Department of
Epidemiology, University of Michigan School of Public Health, Ann
Arbor, Michigan 48109-2029
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