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Mol Microbiol. 1992 May;6(9):1163-72.

Biochemical characterization of Escherichia coli DNA helicase I.

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Department of Biological Sciences, Carnegie-Mellon University, Pittsburgh, Pennsylvania 15213.


The gene product of F tral is a bifunctional protein which nicks and unwinds the F plasmid during conjugal DNA transfer. Further biochemical characterization of the Tral protein reveals that it has a second, much lower, Km for ATP hydrolysis, in addition to that previously identified. Measurement of the single-stranded DNA-stimulated ATPase rate indicates that there is co-operative interaction between the enzyme monomers for maximal activity. Furthermore, 18O-exchange experiments indicate that Tral protein hydrolyses ATP with, at most, a low-level reversal of the hydrolytic step during each turnover.

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