Physical and functional interaction between WRNIP1 and RAD18
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- Yoshimura Akari
- Molecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University
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- Seki Masayuki
- Molecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University
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- Kanamori Makoto
- Molecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University
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- Tateishi Satoshi
- Cell Genetics, Institute of Molecular Embryology and Genetics, Kumamoto University
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- Tsurimoto Toshiki
- Department of Biology Laboratory, School of Sciences, Kyusyu University
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- Tada Shusuke
- Molecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University
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- Enomoto Takemi
- Molecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University Tohoku University 21<sup>st</sup> Century COE program “Comprehensive Research and Education Center for Planning of Drug Development and Clinical Evaluation”
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Abstract
WRN interacting protein 1 (WRNIP1) was originally identified as a protein that interacts with the Werner syndrome responsible gene product (WRN). WRNIP1 is a highly conserved protein from E. coli to humans. Genetic studies in budding yeast suggested that the yeast orthlog of WRNIP1, Mgs1, may function in a DNA damage tolerance pathway that is similar to, but distinct from, the template-switch damage avoidance pathway involving Rad6, Rad18, Rad5, Mms2, and Ubc13. Here we report that human WRNIP1 binds in an ATP dependent manner to both forked DNA that mimics stalled replication forks and to template/primer DNA. We found that WRNIP1 interacts physically with RAD18 and interferes with the binding of RAD18 to forked DNA and to template/primer DNA. In contrast, RAD18 enhances the binding of WRNIP1 to these DNAs, suggesting that WRNIP1 targets DNA bound by RAD18.<br>
Journal
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- Genes & Genetic Systems
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Genes & Genetic Systems 84 (2), 171-178, 2009
The Genetics Society of Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390001205474120320
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- NII Article ID
- 10024791852
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- NII Book ID
- AA11077421
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- ISSN
- 18805779
- 13417568
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- NDL BIB ID
- 10242530
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed