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Originally published In Press as doi:10.1074/jbc.M103588200 on June 4, 2001

J. Biol. Chem., Vol. 276, Issue 34, 31551-31560, August 24, 2001
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Recombinational and Mutagenic Repair of Psoralen Interstrand Cross-links in Saccharomyces cerevisiae*

Ross B. GreenbergDagger , Marie Alberti§, John E. Hearst§, Mark A. ChuaDagger , and Wilma A. SaffranDagger

From the Dagger  Department of Chemistry and Biochemistry, Queens College, City University of New York, Flushing, New York 11367 and the § Department of Chemistry, Lawrence Berkeley National Laboratory, University of California, Berkeley, California 94720

Psoralen photoreacts with DNA to form interstrand cross-links, which can be repaired by both nonmutagenic nucleotide excision repair and recombinational repair pathways and by mutagenic pathways. In the yeast Saccharomyces cerevisiae, psoralen cross-links are processed by nucleotide excision repair to form double-strand breaks (DSBs). In yeast, DSBs are repaired primarily by homologous recombination, predicting that cross-link and DSB repair should induce similar recombination end points. We compared psoralen cross-link, psoralen monoadduct, and DSB repair using plasmid substrates with site-specific lesions and measured the patterns of gene conversion, crossing over, and targeted mutation. Psoralen cross-links induced both recombination and mutations, whereas DSBs induced only recombination, and monoadducts were neither recombinogenic nor mutagenic. Although the cross-link- and DSB-induced patterns of plasmid integration and gene conversion were similar in most respects, they showed opposite asymmetries in their unidirectional conversion tracts: primarily upstream from the damage site for cross-links but downstream for DSBs. Cross-links induced targeted mutations in 5% of the repaired plasmids; all were base substitutions, primarily T right-arrow C transitions. The major pathway of psoralen cross-link repair in yeast is error-free and involves the formation of DSB intermediates followed by homologous recombination. A fraction of the cross-links enter an error-prone pathway, resulting in mutations at the damage site.

* This work was supported in part by grants from the City University of New York PSC-CUNY Research Award Program (to W. A. S.), the National Institutes of Health Grants CA42377 (to W. A. S.) and GM47945 (to J. E. H.), and the Office of Basic Energy Sciences in the Biological Energy division of the Department of Energy under contract number DE-AC03-76SF00098 (to J. E. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The 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: Dept. of Chemistry and Biochemistry, Queens College, City University of New York, 65-30 Kissena Blvd., Flushing, NY 11367. Tel.: 718-997-4195; Fax: 718-997-5531; E-mail: Wilma_Saffran@qc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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