Title |
Visualization of the physical and functional interaction between hMYH and hRad9 by Dronpa bimolecular fluorescence complementation
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Published in |
BMC Molecular and Cell Biology, August 2014
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DOI | 10.1186/1471-2199-15-17 |
Pubmed ID | |
Authors |
Lia Agustina, Soo-Hyun Hahm, Se Hee Han, An Hue Vy Tran, Ji Hyung Chung, Jong-Hwa Park, Jin Woo Park, Ye Sun Han |
Abstract |
Human MutY glycosylase homolog (hMYH), a component of the base excision repair pathway, is responsible for the generation of apurinic/apyrimidinic sites. Rad9-Rad1-Hus1 (9-1-1) is a heterotrimeric protein complex that plays a role in cell cycle checkpoint control and DNA repair. In humans, hMYH and 9-1-1 interact through Hus1 and to a lesser degree with Rad1 in the presence of DNA damage. In Saccharomyces pombe, each component of the 9-1-1 complex interacts directly with SpMYH. The glycosylase activity of hMYH is stimulated by Hus1 and the 9-1-1 complex and enhanced by DNA damage treatment. Cells respond to different stress conditions in different manners. Therefore, we investigated whether Rad9 interacted with hMYH under different stresses. Here, we identified and visualized the interaction between hRad9 and hMYH and investigated the functional consequences of this interaction. |
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