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J Biol Chem, Vol. 273, Issue 11, 6292-6296, March 13, 1998

The DNA-dependent ATPase Activity of Yeast Nucleotide Excision Repair Factor 4 and Its Role in DNA Damage Recognition

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  Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas 78245

Saccharomyces cerevisiae RAD7 and RAD16 genes function together in the nucleotide excision repair of transcriptionally inactive DNA. The RAD7- and RAD16-encoded proteins exist as a tight complex named nucleotide excision repair factor 4 or NEF4. Previously, we showed that NEF4 binds UV-damaged DNA with high specificity and with a dependence upon ATP and that inclusion of NEF4 to the reconstituted nucleotide excision repair system consisting of purified NEF1, NEF2, NEF3, and replication protein A results in marked stimulation of damage-specific DNA incision. Here we show that NEF4 possesses an ATPase activity that is entirely dependent on a DNA cofactor and that double-stranded DNA is twice as effective as single-stranded DNA in activating ATP hydrolysis. Even though DNA binding is promoted by the nonhydrolyzable ATP analogue adenosine 5'-O-(thiotriphosphate) (ATPgamma S), damage binding is more proficient with ATP than with ATPgamma S. Interestingly, UV irradiation of double-stranded DNA results in a pronounced attenuation of the ATPase activity. Taken together, our results suggest a model in which ATP hydrolysis by NEF4 fuels the translocation of NEF4 on DNA in search of UV lesions and damage binding by NEF4 leads to a down-regulation of the ATPase activity. Damage-bound NEF4 could then serve as a nucleation point for the assembly of other repair components.

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