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Nucleic Acids Research, 1991, Vol. 19, No. 23 6413-6418
© 1991

MOLECULAR BIOLOGY

Ca2+-mediated inhibition of a nuclear protein that recognizes UV-damaged DNA and is constitutively overexpressed in resistant human cells: DNA-binding assay

Chuck C.-K. Chao, Shang-Lang Huang and Sue Lin-Chao1

Tumor Biology Laboratory, Departments of Biochemistry and Medicine, Chang Gung Medical College Taoyuan, Taiwan 33332 1Institute of Molecular Biology, Academic Sinica Taipei 11529, Taiwan, Republic of China

Received September 18, 1991. Accepted October 31, 1991.

A nuclear protein that recognizes UV-damaged DNA was detected from HeLa cells using DNA-binding assay. Treatment of cells with Ca2+ ionophore (A23187) caused a dramatic inhibition of the damage-recognition activity. In contrast, in vitro treatment of nuclear extracts with agents that affect protein conformation (such as urea, NP40 and Ca2+) did not significantly affect on the damage-recognition activity. The Ca2+-mediated inhibition of UV damage recognition was reconstituted by the addition of the cytosolic extracts, suggesting that the Ca2+ effect does not directly act on the UV damage-recognition protein. The expression of the detected nuclear protein was increased in UV-resistant HeLa cells. In contrast, the level of this protein was dramatically reduced in UV-sensitive xeroderma pigmentosum group A cells. In addition, UV damage-recognition protein is resistant to RNase, and is independent of the previously identified proteins that bind cisplatin-DNA adduct. These findings implied that the recognition of UV-DNA adduct is modulated by the intracellular level of Ca2+.


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