Phenomenology and Genetic Control of Mitotic Recombination in Yeast

Kunz, Bernard A.; Haynes, Robert H.

doi:10.1146/annurev.ge.15.120181.000421

Cited by 149 publications

(59 citation statements)

References 26 publications

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“…These illegitimate processes include DMA-end joining (also termed end-to-end joining) which results in covalent joining of all kinds of noncomplementary DMA-termini. Examples of homologous recombination include alleleshuffling during sexual DMA exchanges (in prokaryotes; Lederberg and Tatum, 1946) and during meiosis (in eukaryotes; Stahl, 1979), sister chromatid exchange (Latt, 1981) and interchromosomal recombination during mitosis (Kunz and Haynes, 1981;Wasmuth and Vock, 1984). Nonhomologous events play an important role in chromosomal translocations and rearrangements (Gerondakis et a/., 1984;Meuth, 1989), transpositions of retroviruses and transposable elements (Shapiro, 1983), the integration of viral DMA into chromosomes (Gahlmann and Doerfler, 1983), the rearrangement of immunoglobulin and T-cell receptor genes (Honjo, 1983;Malissen etal., 1984;Yanagi et a/., 1984) and the class switching of antibody heavy chain genes (Davis et a/., 1980).…”

Section: Introductionmentioning

confidence: 99%

Dramatic Changes in the Ratio of Homologous Recombination to Nonhomologous DNA-End Joining in Oocytes and Early Embryos ofXenopus laevis

Hagmann¹,

Adlkofer²,

Pfeiffer³

et al. 1996

Biological Chemistry Hoppe-Seyler

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We have developed a versatile plasmid vector (pReco80% of the homologously recombined product, whereas in eggs a highly efficient DMA-end joining activity predominates Both reactions, homologous recombination and DMA-end joining, are shown to occur quickly, with the majority of the respective products being formed within the first 20 minutes of incubation under optimal conditions. In fertilized eggs, up to 50% of all injected linear DMA molecules are recircularized by DMA-end joining. With high amounts of injected DMA per fertilized egg, DMA-end joining is reduced, presumably due to competition for essential factors, and homologous recombination becomes readily detectable.As there is a sequence of rapid cleavage divisions after fertilization of the egg, the fast and highly efficient DMA-end joining, even though it is error-prone at the junction site, seems to be best suited to cope 1 present address: Institut für Zellbiologie, Swiss Federal Institute of Technology, Zürich-Hönggerberg, CH-8093 Zürich, Switzerland with DMA double-strand breaks that might occur in the genome during early embryogenesis. On the other hand, the long-lived oocytes seem to repair DMA double-strand breaks via homologous recombination. This latter property may be exploited both in Xenopus and in other organisms to achieve homologous integration of exogenous DMA into germ cells for gene targeting.

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Section: Introductionmentioning

confidence: 99%

Dramatic Changes in the Ratio of Homologous Recombination to Nonhomologous DNA-End Joining in Oocytes and Early Embryos ofXenopus laevis

Hagmann¹,

Adlkofer²,

Pfeiffer³

et al. 1996

Biological Chemistry Hoppe-Seyler

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“…The RAD51 gene of Saccharomyces cerevisiae is involved in recombination and recombinational repair (for a review, see reference 19). It encodes a protein with homologies to the bacterial RecA proteins (1,3,36).…”

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confidence: 99%

Semidominant Mutations in the Yeast Rad51 Protein and Their Relationships with the Srs2 Helicase

Chanet

Heude

Adjiri

et al. 1996

Molecular and Cellular Biology

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Suppressors of the methyl methanesulfonate sensitivity of Saccharomyces cerevisiae diploids lacking the Srs2 helicase turned out to contain semidominant mutations in Rad51, a homolog of the bacterial RecA protein. The nature of these mutations was determined by direct sequencing. The 26 mutations characterized were single base substitutions leading to amino acid replacements at 18 different sites. The great majority of these sites (75%) are conserved in the family of RecA-like proteins, and 10 of them affect sites corresponding to amino acids in RecA that are probably directly involved in ATP reactions, binding, and/or hydrolysis. Six mutations are in domains thought to be involved in interaction between monomers; they may also affect ATP reactions. By themselves, all the alleles confer a rad51 null phenotype. When heterozygous, however, they are, to varying degrees, negative semidominant for radiation sensitivity; presumably the mutant proteins are coassembled with wild-type Rad51 and poison the resulting nucleofilaments or recombination complexes. This negative effect is partially suppressed by an SRS2 deletion, which supports the hypothesis that Srs2 reverses recombination structures that contain either mutated proteins or numerous DNA lesions.The RAD51 gene of Saccharomyces cerevisiae is involved in recombination and recombinational repair (for a review, see reference 19). It encodes a protein with homologies to the bacterial RecA proteins (1,3,36). These homologies are localized in the regions that form the hydrophobic core of the RecA protein, containing the ATPase and DNA binding domains, as deduced from the three-dimensional structure of the molecule (38-40).Rad51 forms with double-stranded (ds) DNA (27) and single-stranded (ss) DNA (42) filaments similar in structure to those observed with RecA. In the presence of the Rpa DNAbinding proteins, it catalyzes the homologous DNA strand exchange reaction (41,42). Three other S. cerevisiae genes, RAD55 (20), RAD57 (16), and DMC1 (7), also code for proteins with homologies to the ATPase domain of RecA. RAD51, RAD55, and RAD57 belong to the RAD52 epistasis group of genes involved in the repair of ionizing radiation (10) and are part of the same homologous recombination pathway (29). These proteins may well be part of a multiprotein complex: Rad51 interacts with Rad52 in vitro (36) and in vivo (24); it also interacts with Rad55, which in turn interacts with Rad57 (11,15). DMC1 is expressed only during meiosis and is involved in meiotic recombination (7). The Dmc1 and Rad51 proteins appear to be associated in recombination complexes (6). Homologs of Rad51 have also been identified in two other yeasts, Kluyveromyces lactis (9) and Schizosaccharomyces pombe (14, 35), in Neurospora crassa (8), and in higher eucaryotes, including Xenopus laevis (21), chicken (5), mouse (26,35), and human cells (35). In all cases, the regions of greatest homology are confined to the ATPase and DNA binding domains. The human protein forms nucleofilaments with both ss and ds DNAs (4).In ...

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“…Mutations in the DNA repair genes RAD1, RADi0, and RAD52 each lower the frequency of DEL recombination about 4-fold (11,30). The RAD52 gene product is involved in double-strand break repair, in ICR and in meiotic recombination (31). The RAD1 and RAD10 gene products are involved in excision repair and have been shown to have no effect on interchromosomal recombination or meiotic recombination.…”

Section: Resultsmentioning

confidence: 99%

Nonmutagenic carcinogens induce intrachromosomal recombination in dividing yeast cells.

Schiestl

1993

Environ Health Perspect

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Phenomenology and Genetic Control of Mitotic Recombination in Yeast

Cited by 149 publications

References 26 publications

Dramatic Changes in the Ratio of Homologous Recombination to Nonhomologous DNA-End Joining in Oocytes and Early Embryos ofXenopus laevis

Dramatic Changes in the Ratio of Homologous Recombination to Nonhomologous DNA-End Joining in Oocytes and Early Embryos ofXenopus laevis

Semidominant Mutations in the Yeast Rad51 Protein and Their Relationships with the Srs2 Helicase

Nonmutagenic carcinogens induce intrachromosomal recombination in dividing yeast cells.

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