Linked Life Data

11016845

Source:http://linkedlifedata.com/resource/pubmed/id/11016845

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2000-10-26
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0026-8925
pubmed:author
pubmed:issnType
Print
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
154-63
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11016845-Alkylating Agents, pubmed-meshheading:11016845-Amino Acid Sequence, pubmed-meshheading:11016845-Cloning, Molecular, pubmed-meshheading:11016845-DNA Helicases, pubmed-meshheading:11016845-DNA Repair Enzymes, pubmed-meshheading:11016845-Epistasis, Genetic, pubmed-meshheading:11016845-Fungal Proteins, pubmed-meshheading:11016845-Gene Expression Regulation, Fungal, pubmed-meshheading:11016845-Methyl Methanesulfonate, pubmed-meshheading:11016845-Methylnitronitrosoguanidine, pubmed-meshheading:11016845-Molecular Sequence Data, pubmed-meshheading:11016845-Mutagens, pubmed-meshheading:11016845-Mutation, pubmed-meshheading:11016845-Neurospora crassa, pubmed-meshheading:11016845-Saccharomyces cerevisiae, pubmed-meshheading:11016845-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11016845-Sequence Homology, Amino Acid, pubmed-meshheading:11016845-Ultraviolet Rays
pubmed:year
2000
pubmed:articleTitle
Characterization of the Neurospora crassa mus-25 mutant: the gene encodes a protein which is homologous to the Saccharomyces cerevisiae Rad54 protein.
pubmed:affiliation
Department of Regulation Biology, Faculty of Science, Saitama University, Urawa, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't