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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Exhibition Hall 2+3 |
| Time |
10월 19일 (목요일) 11:00~12:30 |
| Code |
BIO.P-254 |
| Subject |
Catalytic roles of zinc finger proteins with structural integration |
| Authors |
Seung Jae Lee*, Yeo Reum Park
Department of Chemistry, Chonbuk National University, Korea
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| Abstract |
Zinc finger (ZF) proteins use zinc as a structural co-factor and are often involved in nucleic acid recognition and binding. Although zinc is typically thought to be the physiologically relevant transition-metal ion for ZF protein function, there is evidence that other metal ions, including iron, may replace zinc under certain conditions. Studies focused on the roles of metal coordination and DNA binding for two specific ZF proteins: ST18 (suppression of tumorogenecity 18) and ZIF268 (zinc interacting factor 268) will be presented.
ST18 is a non-classical ZF that belongs to the NZF/MyT family of ZFs. It contains six ZF domains, each of which has a Cys2His2Cys motif. The biological function of ST18 is not well understood; however, there is some recent evidence that ST18 regulates inflammation and apoptosis by regulating gene expression of tumor necrosis factor-alpha (TNF-α). We have been studying constructs of ST18 that contain the Cys2His2Cys domains, and have obtained evidence for zinc binding. These studies along with DNA binding studies with the TNF-α promoter will be presented.
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| E-mail |
parkyr@jbnu.ac.kr |
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120th General Meeting of the KCS