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A more recent version of this article appeared on October 27, 2000
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Papers In Press, published online ahead of print August 2, 2000
J. Biol. Chem, 10.1074/jbc.M005495200
Submitted on June 22, 2000
Revised on August 1, 2000
Accepted on August 2, 2000

The delta Subunit of DNA Polymerase III Holoenzyme Serves as the Sliding Clamp Unloader in E. col

Frank P. Leu, Manju M. Hingorani, Jennifer Turner, and Mike E. O'Donnell

Laboratory of DNA Replication, The Rockefeller University, New York, NY 10021

Corresponding Author: odonnel{at}rockvax.rockefeller.edu

In E. coli, the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. When synthesis is complete, polymerase dissociates from beta and DNA and cycles to a new start site?primed template loaded with beta . DNA polymerase cycles frequently during lagging strand replication while synthesizing 1-2 kb Okazaki fragments. The clamps left behind remain stable on DNA (t1/2 ~ 100 min), and must be removed rapidly for reuse at numerous primed sites on the lagging strand. Here we show that delta , a single subunit of DNA polymerase III holoenzyme, opens beta and slips it off DNA (kunloading = 0.011 s-1) at a rate similar to that of the multi-subunit gamma complex clamp loader by itself (0.015 s-1) or within Pol III* (~ 0.0065 s-1). Moreover, unlike gamma complex and Pol III*, delta does not require ATP to catalyze clamp unloading. Quantitation of gamma complex subunits (gamma , delta , delta ', chi , psi ) in E. coli cells reveals an excess of delta , free from gamma complex and Pol III*. Since Pol III* and gamma complex occur in much lower quantities, and perform several DNA metabolic functions in replication and repair, the delta subunit likely aids beta clamp recycling during DNA replication.


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