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J. Biol. Chem., Vol. 279, Issue 11, 9857-9866, March 12, 2004

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Transcription Factors NF-YA Regulate the Induction of Human OGG1 Following DNA-alkylating Agent Methylmethane Sulfonate (MMS) Treatment^*

Mi-Rha Lee, Soo-Hyun Kim, Hyun-Ju Cho, Kun-Yeong Lee, Ae Ran Moon, Hye Gwang Jeong, Jung-Sup Lee, Jin-Won Hyun, Myung-Hee Chung¶, and Ho Jin You||**

From the Research Center for Proteineous Materials, Chosun University, 375 Seosuk-dong, Gwangju 501-759, Korea, the ^||Department of Pharmacology, School of Medicine, Chosun University, 375 Seosuk-dong, Gwangju 501-759, Korea, the Department of Biochemistry, College of Medicine Cheju National University, Jeju, Jeju-do, Korea, and the ^¶Department of Pharmacology, Seoul National University College of Medicine, 28 Yongon-dong, Seoul 110-799, Korea

A human 8-oxoguanine-DNA glycosylase (hOGG1) is the main enzyme that repairs 8-oxoG, which is a critical mutagenic lesion. There is a great deal of interest in the up- or down-regulation of OGG1 expression after DNA damage. In this study, we investigated the effect of a DNA-alkylating agent, methylmethane sulfonate (MMS), on hOGG1 expression level and found that MMS treatment resulted in an increase in the functional hOGG1 expression in HCT116 cells. A region between –121 and –61 of the hOGG1 promoter was found to be crucial for this induction by MMS. Site-directed mutations of the two inverted CCAAT motifs substantially abrogated the induction of the hOGG1 promoter as a result of MMS treatment. In addition, the NF-YA protein (binding to the inverted CCAAT box) was induced after exposing cells to MMS. Moreover, gel shift and supershift analyses with the nuclear extracts prepared from HCT116 cells identified NF-YA as the transcription factor interacting with the inverted CCAAT box. Mutations of the inverted CCAAT box either prevented the binding of this factor or abolished its activation as a result of MMS treatment. Finally, this study showed that hOGG1-expressing HCT116 cells exhibited increased hOGG1 repair activity and resistance to MMS. Overall, these results demonstrate that MMS can up-regulate hOGG1 expression through the induction of the transcription factor, NF-YA, and increased transcription level of the hOGG1 gene correlates with an increase in enzyme activity providing functional protection from MMS.

Received for publication, October 9, 2003 , and in revised form, November 24, 2003.

^* This work was supported by the Ministry of Science and Technology of Korea and the KOSEF through the Research Center for Proteineous Materials, and by research funds from Chosun University, 2002. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence should be addressed. Tel.: 82-62-230-6337; Fax: 82-62-233-3720; E-mail: hjyou{at}mail.chosun.ac.kr.

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