A novel proteomic approach identifies new interaction partners for proliferating cell nuclear antigen
|Author(s)||Mesiet Cladiere L2, 3, Norais Cédric2, 3, Kuhn Joelle2, 3, Briffotaux Julien1, Sloostra Jerry W.4, Ferrari Elena5, Hubscher Ulrich5, Flament Didier1, Myllykallio Hannu2, 3|
|Affiliation(s)||1 : IFREMER, Ctr Brest, UMR 6197, Lab Microbiol Environm Extremes, F-29280 Plouzane, France.
2 : Univ Paris 11, CNRS, UMR 8621, F-91405 Orsay, France.
3 : Univ Paris 11, Inst Genet & Microbiol, F-91405 Orsay, France.
4 : Pepscan Syst, NL-8219 PH Lelystad, Netherlands.
5 : Univ Zurich, Inst Vet Biochem & Mol Biol, CH-8057 Zurich, Switzerland.
|Source||Journal of Molecular Biology (0022-2836) (Elsevier), 2007-10 , Vol. 372 , N. 5 , P. 1137-1148|
|WOS© Times Cited||34|
|Keyword(s)||Ribonuclease HII, Combinatorial peptide synthesis, PCNA|
|Abstract||During DNA replication and repair, many proteins bind to and dissociate in a highly specific and ordered manner from proliferating cell nuclear antigen (PCNA). We describe a combined approach of in silico searches at the genome level and combinatorial peptide synthesis to investigate the binding properties of hundreds of short PCNA-interacting peptides (PIP-peptides) to archaeal and eukaryal PCNAs. Biological relevance of our combined approach was demonstrated by identification an inactive complex of Pyrococcus abyssi ribonuclease HII with PCNA. Furthermore we show that PIP-peptides interact with PCNA largely in a sequence independent manner. Our experimental approach also identified many so far unidentified PCNA interacting peptides in a number of human proteins. (c) 2007 Elsevier Ltd. All rights reserved.|