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 p21WAF1/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, incl...

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Bibliographic Details
Published in:Nucleic acids research 1998-09, Vol.26 (17), p.3925-3932
Main Authors: Warbrick, Emma, Lane, David P., Glover, David M., Heatherington, Wayne
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Consensus Sequence
Conserved Sequence
DNA Glycosylases
DNA Ligase ATP
DNA Ligases - genetics
Drosophila
Drosophila melanogaster
Drosophila Proteins
Enzyme-Linked Immunosorbent Assay
Insect Proteins - genetics
Insect Proteins - metabolism
Molecular Sequence Data
N-Glycosyl Hydrolases - genetics
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Peptide Fragments - metabolism
Proliferating Cell Nuclear Antigen - metabolism
Protein Binding
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Transposases - genetics
Transposases - metabolism
Uracil-DNA Glycosidase
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Summary:The eukaryotic polymerase processivity factor, PCNA, interacts with cell cycle regulatory proteins such as p21WAF1/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 p21WAF1/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 PCNAbinding domain as a predictor of PCNA-binding capacity.
ISSN:0305-1048
1362-4962
1362-4962
DOI:10.1093/nar/26.17.3925