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J Biol Chem, Vol. 273, Issue 47, 31541-31546, November 20, 1998

Affinity of Yeast Nucleotide Excision Repair Factor 2, Consisting of the Rad4 and Rad23 Proteins, for Ultraviolet Damaged DNA

Sami N. Guzder, Patrick SungDagger , Louise Prakash, and Satya Prakash

From the Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas 77555-1061 and Dagger  Department of Molecular Medicine/Institute of Biotechnology, University of Texas Health Science Center, San Antonio, Texas 78245

Saccharomyces cerevisiae Rad4 and Rad23 proteins are required for the nucleotide excision repair of UV light-damaged DNA. Previous studies have indicated that these two DNA repair proteins are associated in a tight complex, which we refer to as nucleotide excision repair factor 2 (NEF2). In a reconstituted nucleotide excision repair reaction, incision of UV-damaged DNA is dependent on NEF2, indicating a role of NEF2 in an early step of the repair process. NEF2 does not, however, possess an enzymatic activity, and its function in the damage-specific incision reaction has not yet been defined. Here we use a DNA mobility shift assay to demonstrate that NEF2 binds specifically to UV-damaged DNA. Elimination of cyclobutane pyrimidine dimers from the UV-damaged DNA by enzymatic photoreactivation has little effect on the affinity of NEF2 for the DNA, suggesting that NEF2 recognizes the 6-(1,2)-dihydro-2-oxo-4-pyrimidinyl)-5-methyl-2,4-(1H,3H)-pyrimidinedione photoproducts in the damaged DNA. These results highlight the intricacy of the DNA damage-demarcation reaction during nucleotide excision repair in eukaryotes.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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