Deoxyribonucleic acid repair in the yeast Saccharomyces cerevisiae.

Friedberg, Errol C.

doi:10.1128/mmbr.52.1.70-102.1988

Cited by 179 publications

(72 citation statements)

References 171 publications

(267 reference statements)

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“…That such sensitivity results from a progression rather than a repair defect is suggested by the responses of the other (G2 arrest proficient) rad mutants. By analogy with the budding yeast radiosensitive mutants (Friedberg, 1988), all such mutants are likely to be repair deficient, but all except rad4-llC (Figure 7) showed the same sensitivity for killing as the wild-type. The radl-] mutation sensitized cells to killing by inactivation of DNA ligase.…”

Section: Loss Of Coupling Between the Completion Of Dna Synthesis Andmentioning

confidence: 96%

“…Advances have been made in the study of cellular responses to radiation through the use of radiosensitive mutants, particularly of the budding yeast Saccharomyces cerevisiae (Friedberg, 1988). Radiosensitive mutants of the fission yeast Schizosaccharomyces pombe have been less thoroughly investigated, but the existence of 23 such mutants (Phipps et al, 1985;Lieberman et al, 1989) together with the extensive genetic and molecular understanding of the mitotic control of the fission yeast (Fantes, 1989) make this an ideal system for the study of one aspect of the radiation response -radiation-induced G2 delay.…”

Section: Introductionmentioning

confidence: 99%

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Checkpoint controls in Schizosaccharomyces pombe: rad1.

1992

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‘Checkpoint’ controls ensure that the events of the cell cycle are completed in an orderly fashion. For example, such controls delay mitosis until DNA synthesis and repair of radiation‐induced DNA damage are complete. The rad series of radiosensitive fission yeast mutants was examined to identify strains deficient for the DNA damage‐responsive checkpoint control. Five were identified. A characterization of one (rad1‐1) and the wild‐type is presented. The rad1‐1 mutant does not arrest after irradiation, is sensitive to killing by radiation and is not arrested by hydroxyurea, and thus is also deficient for the DNA synthesis‐responsive checkpoint control. The radiosensitivity of the rad1‐1 mutant was greatly reduced when irradiated and maintained for 6 h in a non‐dividing (density inhibited) state, demonstrating that rad1‐1 is repair proficient and radiosensitive only through failure to delay. The checkpoint controls for which rad1 is required appear to regulate G2‐M progression through the activity of cdc2, here implicated in this role by the coincidence of the radiation transition point and the cdc2 execution point.

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Section: Loss Of Coupling Between the Completion Of Dna Synthesis Andmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Checkpoint controls in Schizosaccharomyces pombe: rad1.

1992

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“…RAD51 is a member of the yeast RAD52 epistasis group that is involved in mitotic and meiotic recombination and DNA repair (Resnick 1987;Friedberg 1988;Petes et al 1991). The RAD51 gene has been cloned from budding yeast and its product is shown to be structurally homologous to RecA of Escherichia coli (Shinohara et al 1992).…”

Section: Introductionmentioning

confidence: 99%

Newt RAD51: Cloning of cDNA and analysis of gene expression during spermatogenesis

Yamamoto¹,

Hikino²,

Nakayama

et al. 1999

Dev Growth Differ

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Animals and reagentsAdult male newts (C. pyrrhogaster) collected during winter and early spring, were purchased from Hamamatsu Seibutsu Kyozai Ltd, Hamamatsu, Japan. Adult female newts were collected during autumn. All chemicals were obtained from Nacalai, Kyoto, Japan, unless otherwise stated. A cDNA encoding a newt homolog of Escherichia coli RecA and yeast RAD51 from a testis cDNA library was isolated. The newt RAD51 (nRAD51) cDNA predicted a 337 amino acid protein with a 95-96% amino acid identity to Xenopus and mammalian RAD51. Northern blot analysis showed that nRAD51 mRNA, 1.7 kb in length, was expressed strongly in the testis and ovary, but weakly in the liver, kidney and brain. In situ hybridization revealed that expression of nRAD51 mRNA was barely observed in primary spermatogonia (one cell in a cyst) and early secondary spermatogonia (two to four cells in a cyst), but increased in late secondary spermatogonia (≥ eight cells in a cyst), reaching a maximum level in leptotene-zygotene spermatocytes, and thereafter declined. These results suggest that nRAD51 is involved in mitotic recombination in spermatogonia as well as in meiotic recombination in spermatocytes.

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“…A large number of DNA alkylation sensitive mutants have been identified in Saccharomyces cerevisiae (Friedberg, 1988) and more than a dozen alkylation inducible genes have been found (Johnston and Nasmyth, 1978;McClanahan and McEntee, 1984;Ruby et al, 1983;Peterson et al, 1985;Ruby and Szostack, 1985; Madura and Prakash, 1986;Robinson et al, 1986;Cole et al, 1987;Hurd et al, 1987;Treger et al, 1988;Davis, 1987, 1989), but so far the products of only three of these inducible genes have been identified, namely, DNA ligase (Johnston and Nasmyth, 1978;Peterson et al, 1985), ribonucleotide reductase (Hurd et al, 1987;Davis, 1987, 1989) and ubiquitin (Treger et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to the AlkA glycosylase of E. coli and is induced in response to DNA alkylation damage.

1990

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We previously cloned a DNA fragment from Saccharomyces cerevisiae that suppressed the alkylation sensitivity of Escherichia coli glycosylase deficient mutants and we showed that it apparently contained a gene for 3‐methyl‐adenine DNA glycosylase (MAG). Here we establish the identity of the MAG gene by sequence analysis and describe its in vivo function and expression in yeast cells. The MAG DNA glycosylase specifically protects yeast cells against the killing effects of alkylating agents. It does not protect cells against mutation; indeed, it appears to generate mutations which presumably result from those apurinic sites produced by the glycosylase that escape further repair. The MAG gene, which we mapped to chromosome V, is not allelic with any of the RAD genes and appears to be allelic to the unmapped MMS‐5 gene. From its sequence the MAG glycosylase is predicted to contain 296 amino acids and have a molecular weight of 34,293 daltons. A 137 amino acid stretch of the MAG glycosylase displays 27.0% identity and 63.5% similarity with the E. coli AlkA glycosylase. Transcription of the MAG gene, like that of the E. coli alkA gene, is greatly increased when yeast cells are exposed to relatively non‐toxic levels of alkylating agents.

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Deoxyribonucleic acid repair in the yeast Saccharomyces cerevisiae.

Cited by 179 publications

References 171 publications

Checkpoint controls in Schizosaccharomyces pombe: rad1.

Checkpoint controls in Schizosaccharomyces pombe: rad1.

Newt RAD51: Cloning of cDNA and analysis of gene expression during spermatogenesis

Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to the AlkA glycosylase of E. coli and is induced in response to DNA alkylation damage.

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