A novel proteomic approach identifies new interaction partners for proliferating cell nuclear antigen
A novel proteomic approach identifies new interaction partners for proliferating cell nuclear antigen
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DOI：
10.1016/j.jmb.2007.06.056
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发表时间：
2007-10-05
影响因子：
5.6
通讯作者：
Myllykallio, Hannu
中科院分区：
文献类型：
--
作者：
Mesiet-Cladiere, Laurence;Norais, Cedric;Myllykallio, Hannu
在DNA复制和修复过程中，许多蛋白质以高度特异性和有序的方式与增殖细胞核抗原（PCNA）结合和分离。我们描述了一种组合方法，在基因组水平上进行计算机搜索和组合肽合成，以研究数百种短的pcna相互作用肽（pip肽）与古细菌和真核细菌pcna的结合特性。我们的联合方法的生物学相关性被证明是通过鉴定与PCNA的深海焦球菌核糖核酸酶HII的无活性复合体。此外，我们发现pip肽与PCNA的相互作用在很大程度上与序列无关。我们的实验方法还在许多人类蛋白质中鉴定了许多迄今为止尚未鉴定的PCNA相互作用肽。(c) 2007 Elsevier Ltd.版权所有。
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.