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JBC, Vol. 253, Issue 9, 3298-3304, May, 1978
A. Kornberg, J. F. Scott and L. L. Bertsch
Hydrolysis of ATP by rep protein proceeds in the presence of a
single-stranded region of DNA 4 residues long, but the true effector for
rep ATPase appears to be a replicating fork rather than a random coil. At
or near a fork in duplex DNA, rep ATPase action is different from what it
is on DNA lacking secondary structure (single-stranded): (i) Km for ATP is
lower, (ii) specificity is for ATP and dATP with no action on other
nucleoside triphosphates, (iii) sensitivity to certain ATP analogs is
reduced, (iv) presence of a DNA-nicking enzyme (e.g. cistron A protein
induced by phiX174) is required, and (v) Escherichia coli DNA binding
protein facilitates rather than inhibits. During the separation of strands
accompanying replication, 2 molecules of nucleoside triphosphate (ATP or
dATP) are hydrolyzed for every nucleotide polymerized. Utilization of ATP
by rep protein may provide energy for catalytic strand separation at a fork
in advance of replication.
ATP utilization by rep protein in the catalytic separation of DNA strands at a replicating fork
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