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(Received for publication, April 11, 1996)
From the We have shown previously that a protein-protein
interaction between DnaG and DnaB is required to attract the primase to
the replication fork. This interaction was mediated by the C-terminal
16-kDa domain (p16) of the primase. A screen was developed that allowed
the detection of mutant p16 proteins that did not interact with DnaB.
Various mutagenesis protocols were used to localize this interaction
domain to the extreme C terminus of the primase. A mutant primase
missing only the C-terminal 16 amino acids was isolated and its
activities examined. This mutant enzyme was fully active as a primase,
but was incapable of interacting with DnaB. Thus, the mutant primase
could not support DNA synthesis in either the general priming reaction
or during
Volume 271, Number 35,
Issue of August 30, 1996
pp. 21391-21397
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
and§
Graduate Program in Molecular Biology,
Cornell University Graduate School of Medical Sciences, New York, New
York 10021 and the § Molecular Biology Program, Memorial
Sloan-Kettering Cancer Center, New York, New York 10021
X174 complementary strand DNA replication. Alanine cluster
mutagenesis and deletion analysis in p16 allowed the further
localization of the interaction domain to the extreme C-terminal 8 amino acids in primase.
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