mei-3, a recombination and repair gene of Neurospora crassa, encodes a RecA-like protein

Cheng, Richard Z.; Baker, T. I.; Cords, Carl E.; Radloff, Roger

doi:10.1016/0921-8777(93)90005-2

Cited by 41 publications

(17 citation statements)

References 24 publications

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“…1). As starting probe we used the pooled NotI DNA inserts from cosmids 9:1H and 9:7G, which contain the gene mei-3 (Cheng et al, 1993). A total of 11 cosmid clones (100 kb) were cloned around mei-3 (contig MEI-3; Fig.…”

Section: Construction Of the Mei-3 And His-2 Cosmid Contigsmentioning

confidence: 99%

Mapping Chromosome Landmarks in the Centromere I Region ofNeurospora crassa

Rosa

Haedo

Temporini

et al. 1997

Fungal Genetics and Biology

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Section: Construction Of the Mei-3 And His-2 Cosmid Contigsmentioning

confidence: 99%

Mapping Chromosome Landmarks in the Centromere I Region ofNeurospora crassa

Rosa

Haedo

Temporini

et al. 1997

Fungal Genetics and Biology

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“…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.…”

mentioning

confidence: 90%

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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“…Two of the genes involved, mei-3 and mus-23, have already been cloned and characterized as counterparts of S. cerevisiae RAD51 and MRE11, respectively (Cheng et al 1993;Hatakeyama et al 1995;Watanabe et al 1997).…”

Section: Introductionmentioning

confidence: 99%

Characterization of the Neurospora crassa mus-25 mutant: the gene encodes a protein which is homologous to the Saccharomyces cerevisiae Rad54 protein

et al. 2000

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Characterization of the Neurospora crassa mus-25 mutant suggests that it is defective in recombination repair and belongs to the uvs-6 epistasis group. It shows a high sensitivity to the alkylating agents methyl methanesulfonate (MMS) and N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), but not to UV radiation. It is barren (i.e. does not produce ascospores) in homozygous crosses. The frequency of MMS-induced mutations at the ad-3 loci is approximately three times higher than in the wild type. The ratio of homologous to nonhomologous integration of the pMTR::HYG plasmid is much lower than in wild type. The mus-25 mutant is epistatic to the mei-3 mutant for MMS sensitivity. mei-3, which is a homololog of the Saccharomyces cerevisiae gene RAD51, is a member of the uvs-6 epistasis group which contains several genes that are homologous to recombination repair genes in other organisms. The mus-25 gene was cloned by identifying a genomic DNA fragment which complements the MMS sensitivity of the mutant. The amino acid sequence deduced from the cloned DNA showed a high degree of homology to the Rad54 protein, which is involved in recombinational repair in S. cerevisiae. Comparison of the nucleotide sequences of the genomic and cDNAs of the mus-25 gene revealed an ORF of 2505 bp with a single 118-bp intron beginning immediately after the second nucleotide of the AUG start codon. The molecular weight of the deduced gene product was 93.5 kDa. The transcript level was raised within 60 min after UV irradiation or MMS treatment, as also observed for the expression of the other N. crassa recombinational repair genes, suggesting the existence of a common mechanism which induces expression of the recombinational repair genes in response to DNA damage.

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mei-3, a recombination and repair gene of Neurospora crassa, encodes a RecA-like protein

Cited by 41 publications

References 24 publications

Mapping Chromosome Landmarks in the Centromere I Region ofNeurospora crassa

Mapping Chromosome Landmarks in the Centromere I Region ofNeurospora crassa

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

Characterization of the Neurospora crassa mus-25 mutant: the gene encodes a protein which is homologous to the Saccharomyces cerevisiae Rad54 protein

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