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Nucleic Acids Research, 1995, Vol. 23, No. 8 1374-1379
© 1995

MOLECULAR BIOLOGY

DNA and RNA-DNA annealing activity associated with the {tau} subunit of the Escherichia coil DNA polymerase III holoenzyme

Sungsub Kim and Kenneth J. Marians*

Molecular Biology Program, Memorial Sloan-Kettering Cancer Center and Graduate Program in Molecular Biology, Cornell University Graduate School of Medical Sciences New York, NY 10021, USA

*To whom correspondence should be addressed

Received December 15, 1994. Revised March 1, 1995. Accepted March 1, 1995.

The DNA polymerase III (pol III)holoenzyme is the 10 subunit replicase of Escherichia coli. The 71 kDa{tau} subunit, encoded by dnaX, dimerizes the core polymerase ({alpha}{varepsilon}{theta}) to form pol III' [({alpha}{varepsilon}{theta})2{tau}2]. {tau} is also a single-stranded DNA-dependent ATPase and can substitute for the {gamma} subunit during initiation complex formation. We show here that {tau} also possessesa DNA-DNA and RNA-DNA annealing activity that is stimulated by Mg2+ but neither requires ATP nor is inhibited by non-hydrolyzable ATP analogs. This suggests the {tau} may act to stabilize the primer-template interaction during DNA replication.


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