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J. Biol. Chem., Vol. 255, Issue 21, 10100-10106, Nov, 1980
RB O'Gorman, M Dunaway and KS Matthews
The nonspecific DNA binding capacity of repressor protein has been assessed
by boundary sedimentation of repressor and calf thymus DNA fragmented by
shearing and by nitrocellulose ultrafiltration employing labeled lambdaplac
DNA in the presence of inducer concentrations sufficient to insure
dissociation of repressor from the operator region of the DNA. These
methods gave values in good agreement with values previously reported in
the literature. The association constants for the interaction of repressor
with operator DNA fragments and lambdaplac DNA have been measured and found
to differ by approximately 100-fold at low salt concentrations, but the
difference decreases to 4-fold at salt concentrations near the
physiological value. The equilibrium association constant for the
repressor-operator DNA fragment is significantly less sensitive to salt
concentration than the corresponding constant for lambdaplac DNA. Inducer
decreases the salt concentration dependence of repressor-operator DNA
fragment only slightly. Measurement of the association constants for the
interaction of the trypsin-resistant core protein with operator DNA
fragment and lambdaplac DNA indicate that the core protein binds to the two
DNA's with the same affinity. This result contrasts with the differential
affinity of intact repressor for these two DNA's. In addition, the core
protein association constants for operator DNA fragment and lambdaplac DNA
display minimal dependence on the salt concentration. These results suggest
a role for nonionic interactions in the binding of core protein to operator
DNA.
DNA binding characteristics of lactose repressor and the trypsin- resistant core repressor
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