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JBC, Vol. 250, Issue 18, 7377-7387, Sep, 1975
A. E. Karu, Y. Sakaki, H. Echols and S. Linn
The protein encoded by the gam gene of bacteriophage lambda ("gamma
protein") is a specific inhibitor of the recBC enzyme of Escherichia coli.
The lambda protein has been purified approximately 2,000-fold, and its
structure and inhibitory activity have been characterized. It appears to be
composed of two identical subunits of 16,500 daltons, inhibits all of the
catalytic activities of the recBC enzyme with apparently equal efficiency,
but has no effect upon any other E. coli or lambda-DNase tested. Inhibition
does not occur unless recBC enzyme is exposed to gamma protein prior to
reaction of the enzyme with DNA. The inhibitory activity is independent of
temperature, and no catalytic activity has been detected that might fulfill
the inhibitory function. It appears instead that the inhibition involves a
stoichiometric, rather than a catalytic interaction between gamma protein
and the enzyme. Reaction kinetics for the recBC enzyme inhibited by gamma
protein show no anomalous protein--only a depressed rate. Inhibition is not
competitive and does not appear to affect the enzyme's affinity for DNA.
The enzyme remains inhibited after it is separated from "excess" gamma
protein by gel filtration or sedimentation in a glycerol gradient, and
inhibited enzyme has a reduced electrophoretic mobility compared to that of
uninhibited enzyme. Gamma Protein inhibits recBC enzyme which has been
reconstituted from cell-free extracts by complementation in vitro, but at
least one of the complementing factors present in extracts from recB- cells
does not by itself form a complex with gamma protein. The mechanism of
inhibition and the implications of these results from gamma replication and
recombination are discussed.
The gamma protein specified by bacteriophage gamma. Structure and inhibitory activity for the recBC enzyme of Escherichia coli
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