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Biochemical characterization of Escherichia coli DNA helicase I

Biochemical characterization of Escherichia coli DNA helicase I Summary 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular Microbiology Wiley

Biochemical characterization of Escherichia coli DNA helicase I

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References (62)

Publisher
Wiley
Copyright
Copyright © 1992 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0950-382X
eISSN
1365-2958
DOI
10.1111/j.1365-2958.1992.tb01555.x
Publisher site
See Article on Publisher Site

Abstract

Summary 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.

Journal

Molecular MicrobiologyWiley

Published: May 1, 1992

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