Expression of the E.coli ada gene in S.cerevisiae provides cellular resistance to N-methyl-N'-nitro-N-nitrosoguanidine in rad6 but not in rad52 mutants.

2.50
Hdl Handle:
http://hdl.handle.net/10541/96215
Title:
Expression of the E.coli ada gene in S.cerevisiae provides cellular resistance to N-methyl-N'-nitro-N-nitrosoguanidine in rad6 but not in rad52 mutants.
Authors:
Brozmanová, J; Vlcková, V; Chovanec, M; Cernáková, L; Skorvaga, M; Margison, Geoffrey P
Abstract:
The Escherichia coli ada gene protein coding region under the control of the yeast alcohol dehydrogenase promoter in the extrachromosomally replicating yeast expression vectors pADHO6C and pVT103LO6C was introduced into the wild-type yeast strains, YNN-27 and FF-18733, and the repair deficient mutants LN-1 (rad1-1), VV-5 (rad6-1), C5-6 (rad52-1) and FF-18742 (rad52::URA3). This resulted in the expression of 3950, 1900, 1870, 1620, 1320 and 1420 fmol ada-encoded ATase/mg protein respectively: transformation with the parent vectors resulted in ATase activities of 3-17 fmol/mg protein. The wild-types, rad1-1 and rad6-1 yeast expressing the bacterial ATase showed increased resistance to the toxic and mutagenic effects of N-methyl-N'-nitro-N- nitrosoguanidine (MNNG). Expression of ATase in the rad52-1 and rad52::URA3 mutants neither complemented their sensitivity, nor reduced the mutagenic effects of this agent. These results suggest that whilst a portion of the toxic and mutagenic lesions induced by MNNG can be repaired in yeast by the E.coli Ada protein in a RAD1- and RAD6-independent manner, the RAD52 gene product may be essential for the complete functioning of the Ada ATase. This is the first suggestion of a possible cofactor requirement for ATase.
Affiliation:
Department of Molecular Genetics, Cancer Research Institute, Slovak Academy of Sciences, Bratislava.
Citation:
Expression of the E.coli ada gene in S.cerevisiae provides cellular resistance to N-methyl-N'-nitro-N-nitrosoguanidine in rad6 but not in rad52 mutants. 1994, 22 (25):5717-22 Nucleic Acids Res.
Journal:
Nucleic Acids Research
Issue Date:
25-Dec-1994
URI:
http://hdl.handle.net/10541/96215
PubMed ID:
7838727
Type:
Article
Language:
en
ISSN:
0305-1048
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorBrozmanová, Jen
dc.contributor.authorVlcková, Ven
dc.contributor.authorChovanec, Men
dc.contributor.authorCernáková, Len
dc.contributor.authorSkorvaga, Men
dc.contributor.authorMargison, Geoffrey Pen
dc.date.accessioned2010-04-09T14:37:30Z-
dc.date.available2010-04-09T14:37:30Z-
dc.date.issued1994-12-25-
dc.identifier.citationExpression of the E.coli ada gene in S.cerevisiae provides cellular resistance to N-methyl-N'-nitro-N-nitrosoguanidine in rad6 but not in rad52 mutants. 1994, 22 (25):5717-22 Nucleic Acids Res.en
dc.identifier.issn0305-1048-
dc.identifier.pmid7838727-
dc.identifier.urihttp://hdl.handle.net/10541/96215-
dc.description.abstractThe Escherichia coli ada gene protein coding region under the control of the yeast alcohol dehydrogenase promoter in the extrachromosomally replicating yeast expression vectors pADHO6C and pVT103LO6C was introduced into the wild-type yeast strains, YNN-27 and FF-18733, and the repair deficient mutants LN-1 (rad1-1), VV-5 (rad6-1), C5-6 (rad52-1) and FF-18742 (rad52::URA3). This resulted in the expression of 3950, 1900, 1870, 1620, 1320 and 1420 fmol ada-encoded ATase/mg protein respectively: transformation with the parent vectors resulted in ATase activities of 3-17 fmol/mg protein. The wild-types, rad1-1 and rad6-1 yeast expressing the bacterial ATase showed increased resistance to the toxic and mutagenic effects of N-methyl-N'-nitro-N- nitrosoguanidine (MNNG). Expression of ATase in the rad52-1 and rad52::URA3 mutants neither complemented their sensitivity, nor reduced the mutagenic effects of this agent. These results suggest that whilst a portion of the toxic and mutagenic lesions induced by MNNG can be repaired in yeast by the E.coli Ada protein in a RAD1- and RAD6-independent manner, the RAD52 gene product may be essential for the complete functioning of the Ada ATase. This is the first suggestion of a possible cofactor requirement for ATase.en
dc.language.isoenen
dc.subject.meshBacterial Proteins-
dc.subject.meshDNA Repair-
dc.subject.meshDNA-Binding Proteins-
dc.subject.meshEscherichia coli-
dc.subject.meshEscherichia coli Proteins-
dc.subject.meshFungal Proteins-
dc.subject.meshGenes, Bacterial-
dc.subject.meshGenes, Fungal-
dc.subject.meshLigases-
dc.subject.meshMethylnitronitrosoguanidine-
dc.subject.meshMethyltransferases-
dc.subject.meshO(6)-Methylguanine-DNA Methyltransferase-
dc.subject.meshRad52 DNA Repair and Recombination Protein-
dc.subject.meshSaccharomyces cerevisiae-
dc.subject.meshSaccharomyces cerevisiae Proteins-
dc.subject.meshTranscription Factors-
dc.subject.meshUbiquitin-Conjugating Enzymes-
dc.titleExpression of the E.coli ada gene in S.cerevisiae provides cellular resistance to N-methyl-N'-nitro-N-nitrosoguanidine in rad6 but not in rad52 mutants.en
dc.typeArticleen
dc.contributor.departmentDepartment of Molecular Genetics, Cancer Research Institute, Slovak Academy of Sciences, Bratislava.en
dc.identifier.journalNucleic Acids Researchen

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