期刊
NUCLEIC ACIDS RESEARCH
卷 29, 期 13, 页码 2802-2809出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/29.13.2802
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资金
- NCI NIH HHS [R01 CA084461, R01-CA84461] Funding Source: Medline
- NIA NIH HHS [R01-AG17432, P01 AG021830] Funding Source: Medline
- NIEHS NIH HHS [P30 ES06676, P30 ES006676] Funding Source: Medline
The human MutY homolog, hMYH, is an adenine-specific DNA glycosylase that removes adenines or 2-hydroxyadenines mispaired with guanines or 8-oxoguanines, In order to prevent mutations, this activity must be directed to the newly synthesized strand and not the template strand during DNA synthesis. The subcellular localization and expression of hMYH has been studied in serum-stimulated, proliferating MRC5 cells. Using specific antibodies, we demonstrate that endogenous hMYH protein localized both to nuclei and mitochondria, hMYH in the nuclei is distinctly distributed and co-localized with BrdU at replication foci and with proliferating cell nuclear antigen (PCNA), The levels of hMYH in the nucleus increased 3- to 4-fold during progression of the cell cycle and reached maximum levels in S phase compared to early G(1). Similar results were obtained for PCNA, while there were no notable changes in expression of 8-oxoguanine glycosylase or the human MutT homolog, MTH1, throughout the cell cycle. The cell cycle-dependent expression and localization of hMYH at sites of DNA replication suggest a role for this glycosylase in immediate postreplication DNA base excision repair.
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