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J. Biol. Chem., Vol. 277, Issue 47, 45331-45337, November 22, 2002
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From the Ludwig Institute for Cancer Research, Cancer Center, and
Department of Medicine, University of California San Diego School
of Medicine, La Jolla, California 92093-0660
Proliferating cell nuclear antigen (PCNA) plays
an essential role in eukaryotic DNA replication, and numerous DNA
replication proteins have been found to interact with PCNA through a
conserved eight-amino acid motif called the PIP-box. We have searched
the genome of the yeast Saccharomyces cerevisiae for open
reading frames that encode proteins with putative PIP-boxes and
initiated testing of 135 novel candidates for their ability to interact with PCNA-conjugated agarose beads. The first new PCNA-binding protein
identified in this manner is the 5' to 3' DNA helicase RRM3. Yeast
two-hybrid tests show that N-terminal deletions of RRM3, which remove
the PIP-box but leave the helicase motifs intact, abolish the
interaction with PCNA. In addition, mutating the two phenylalanine
residues in the PIP-box to alanine or aspartic acid reduces binding to
PCNA, confirming that the PIP-box in RRM3 is responsible for
interaction with PCNA. The results presented here suggest that the RRM3
helicase functions at the replication fork.
Saccharomyces cerevisiae RRM3, a 5' to 3'
DNA Helicase, Physically Interacts with Proliferating Cell Nuclear
Antigen*
*
This project was supported by National Institutes of Health
Grant GM27017 (to R. D. K.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Ludwig Institute for
Cancer Research, University of California San Diego School of Medicine,
CMME 3080, 9500 Gilman Dr., La Jolla, CA 92093-0669. Tel.:
858-534-7804; Fax: 858-534-7750; E-mail: rkolodner@ucsd.edu.
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