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dc.contributor.authorWilkinson, M C
dc.contributor.authorPotter, P M
dc.contributor.authorCawkwell, L
dc.contributor.authorGeorgiadis, P
dc.contributor.authorPatel, D
dc.contributor.authorSwann, P F
dc.contributor.authorMargison, Geoffrey P
dc.date.accessioned2010-09-10T14:59:57Z
dc.date.available2010-09-10T14:59:57Z
dc.date.issued1989-11-11
dc.identifier.citationPurification of the E. coli ogt gene product to homogeneity and its rate of action on O6-methylguanine, O6-ethylguanine and O4-methylthymine in dodecadeoxyribonucleotides. 1989, 17 (21):8475-84 Nucleic Acids Res.en
dc.identifier.issn0305-1048
dc.identifier.pmid2685744
dc.identifier.doi10.1093/nar/17.21.8475
dc.identifier.urihttp://hdl.handle.net/10541/111016
dc.description.abstractThe E. coli gene ogt encodes the DNA repair protein O6-alkylguanine-DNA-alkyltransferase (O6-AlkG ATase). The protein coding region of the gene was cloned into a multicopy expression vector to obtain high yields of the enzyme (approximately 0.2% of total protein) which was purified to apparent homogeneity by affinity, molecular exclusion and reverse-phase chromatography. Good correlation was found between the determined and predicted amino acid compositions. The ability of the purified protein to act on O6-methylguanine (O6-MeG), O6-ethylguanine (O6-EtG) and O4-methylthymine (O4-MeT) in self-complementary dodecadeoxyribonucleotides was compared to that of 19 kDa fragment of the related ada-protein. With both proteins the rate order was O6-MeG greater than O6-EtG greater than O4-MeT, however, the ogt protein was found to repair O6-MeG, O6-EtG and O4-Met, 1.1, 173 and 84 times, respectively, faster than the ada protein.
dc.language.isoenen
dc.subject.meshAlkylating Agents
dc.subject.meshAmino Acids
dc.subject.meshChromatography, High Pressure Liquid
dc.subject.meshDNA Repair
dc.subject.meshDeoxyribonucleotides
dc.subject.meshElectrophoresis, Polyacrylamide Gel
dc.subject.meshEscherichia coli
dc.subject.meshGene Expression
dc.subject.meshGenes, Bacterial
dc.subject.meshGuanine
dc.subject.meshMethylation
dc.subject.meshMethyltransferases
dc.subject.meshO(6)-Methylguanine-DNA Methyltransferase
dc.subject.meshThymine
dc.titlePurification of the E. coli ogt gene product to homogeneity and its rate of action on O6-methylguanine, O6-ethylguanine and O4-methylthymine in dodecadeoxyribonucleotides.en
dc.typeArticleen
dc.contributor.departmentDepartment of Carcinogenesis, Christie Hospital and Holt Radium Institute, Manchester, UK.en
dc.identifier.journalNucleic Acids Researchen
html.description.abstractThe E. coli gene ogt encodes the DNA repair protein O6-alkylguanine-DNA-alkyltransferase (O6-AlkG ATase). The protein coding region of the gene was cloned into a multicopy expression vector to obtain high yields of the enzyme (approximately 0.2% of total protein) which was purified to apparent homogeneity by affinity, molecular exclusion and reverse-phase chromatography. Good correlation was found between the determined and predicted amino acid compositions. The ability of the purified protein to act on O6-methylguanine (O6-MeG), O6-ethylguanine (O6-EtG) and O4-methylthymine (O4-MeT) in self-complementary dodecadeoxyribonucleotides was compared to that of 19 kDa fragment of the related ada-protein. With both proteins the rate order was O6-MeG greater than O6-EtG greater than O4-MeT, however, the ogt protein was found to repair O6-MeG, O6-EtG and O4-Met, 1.1, 173 and 84 times, respectively, faster than the ada protein.


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