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(Received for publication, April 5, 1996, and in revised form, June 15, 1996)
From the Synthesis of an Okazaki fragment occurs once
every 1 or 2 s at the Escherichia coli replication
fork. To account for the rapid recycling required of the lagging-strand
polymerase, it has been proposed that it is held at the replication
fork by protein-protein interactions with the leading-strand polymerase
as part of a dimeric polymerase assembly. Solution studies showed that
the replicative polymerase, the DNA polymerase III holoenzyme, was
indeed a dimer with two catalytic cores held together by the
Volume 271, Number 35,
Issue of August 30, 1996
pp. 21406-21412
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Couples the Leading- and Lagging-strand Polymerases at the
Escherichia coli DNA Replication Fork
,
Graduate Program in Molecular Biology
Cornell University Graduate School of Medical Sciences, New York, New
York 10021, the § Department of Biochemistry, Biophysics,
and Genetics, and Graduate Program in Molecular Biology University of
Colorado Health Sciences Center, Denver, Colorado 80262, and the
Molecular Biology Program, Memorial Sloan-Kettering Cancer
Center, New York, New York 10021
subunit. However, the functionality of this arrangement at the
replication fork has never been demonstrated. We showed previously that
the lagging-strand polymerase acted processively during multiple rounds
of Okazaki fragment synthesis, i.e. the same polymerase
core assembly synthesized each and every fragment made by the fork.
Using extreme dilution of active replication forks and the isolation of
protein-DNA complexes capable of supporting coupled leading- and
lagging-strand synthesis, we demonstrate here that this coupling of
leading- and lagging-strand synthesis is, in fact, mediated by the subunit of the holoenzyme acting as a physical bridge between the core
assemblies synthesizing the leading and lagging strands.
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