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Nucleic Acids Research, 2001, Vol. 29, No. 13 2802-2809
© 2001 Oxford University Press

hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs

Istvan Boldogh, Daun Milligan1, Myung Soog Lee, Heather Bassett1, R. Stephen Lloyd1 and Amanda K. McCullough1,* Department of Microbiology and Immunology and 1Sealy Center for Environmental Health and Medicine, Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX 77555-1071 USA

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 G1. 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 post-replication DNA base excision repair.

* To whom correspondence should be addressed. Tel: +1 409 772 6310; Fax: +1 409 772 1790; Email: akmccull{at}utmb.edu


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