PCNA binding proteins in Drosophila melanogaster : the analysis of a conserved PCNA binding domain.

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.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, Consensus Sequence, Conserved Sequence, DNA Glycosylases, DNA Ligases, Drosophila Proteins, Drosophila melanogaster, Enzyme-Linked Immunosorbent Assay, Insect Proteins, Molecular Sequence Data, N-Glycosyl Hydrolases, Nuclear Proteins, Peptide Fragments, Proliferating Cell Nuclear Antigen, Protein Binding, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Transposases, Uracil-DNA Glycosidase
Nucleic Acids Res.
Date: Sep. 01, 1998
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