RADH , a gene of Saccharomyces cerevisiae encoding a putative DNA helicase involved in DNA repair. Characteristics of radH mutants and sequence of the gene (original) (raw)

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Institut Curie-Biologie, Bätiment 110, Centre Universitaire

91405 Orsay, France

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Institut Curie-Biologie, Bätiment 110, Centre Universitaire

91405 Orsay, France

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1

Faculty of Food and Biotechnology, University of Zagreb

Pierottijeva 6, 41000 Zagreb, Yugoslavia

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Institut Curie-Biologie, Bätiment 110, Centre Universitaire

91405 Orsay, France

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,

Institut Curie-Biologie, Bätiment 110, Centre Universitaire

91405 Orsay, France

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Institut Curie-Biologie, Bätiment 110, Centre Universitaire

91405 Orsay, France

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Revision received:

22 August 1989

Published:

25 September 1989

Cite

Abdelilah Aboussekhra, Roland Chanet, Zoran Zgaga, Corinne Cassier-Chauvat, Martine Heude, Francis Fabre, RADH , a gene of Saccharomyces cerevisiae encoding a putative DNA helicase involved in DNA repair. Characteristics of radH mutants and sequence of the gene , Nucleic Acids Research, Volume 17, Issue 18, 25 September 1989, Pages 7211–7219, https://doi.org/10.1093/nar/17.18.7211
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Abstract

A new type of radiation-sensitive mutant of S. cerevisiae is described. The recessive radH mutation sensitizes to the lethal effect of UV radiations haploids in the G1 but not in the G2 mitotic phase. Homozygous diploids are as sensitive as G1 haploids. The UV-induced mutagenesis is depressed, while the induction of gene conversion is increased. The mutation is believed to channel the repair of lesions engaged in the mutagenic pathway into a recombination process, successful if the events involve sister-chromatids but lethal if they involve homologous chromosomes. The sequence of the RADH gene reveals that it may code for a DNA helicase, with a Mr of 134 kDa. All the consensus domains of known DNA helicases are present. Besides these consensus regions, strong homologies with the Rep and UvrD helicases of E. coli were found. The RadH putative helicase appears to belong to the set of proteins involved in the error-prone repair mechanism, at least for UV-induced lesions, and could act in coordination with the Rev3 error-prone DNA polymerase

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