Nucleic Acids Research, Vol 26, Issue 17 3925-3932, Copyright © 1998 by Oxford University Press
E Warbrick, W Heatherington, DP Lane and DM Glover
The eukaryotic polymerase processivity factor, PCNA, interacts with cell
cycle regulatory proteins such as p21(WAF1/Cip1) and Gadd45, as well as
with proteins involved in the mechanics of DNA repair and replication. A
conserved PCNA-binding motif is found in a subset of PCNA-interacting
proteins, including p21, suggesting that the regulation of these
interactions is important for the co-ordination of DNA replication and
repair. We have identified several classes of protein which bind to
Drosophila PCNA. Two of these proteins contain the consensus PCNA-binding
domain: one is the Dacapo protein, a Drosophila homologue of
p21(WAF1/Cip1), and the second is the transposase encoded by the Pogo DNA
transposon . A conserved PCNA- binding domain is also present in a human
relative of Pogo , named Tigger , suggesting that this domain has a
functional role in this class of transposable element. This raises
interesting possibilities for a novel method of transposition in which the
transposase might be targeted to replicating DNA. Finally, we have
investigated the use of this conserved PCNA-binding domain as a predictor
of PCNA-binding capacity.
ARTICLES
PCNA binding proteins in Drosophila melanogaster : the analysis of a conserved PCNA binding domain
CRC Laboratories, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, UK. ewarbrick@dundee.ac.uk
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