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Site directed mutagenesis of two cysteine residues in the E. coli ogt O6-alkylguanine DNA alkyltransferase protein.

dc.contributor.authorHarris, L C
dc.contributor.authorPotter, P M
dc.contributor.authorMargison, Geoffrey P
dc.date.accessioned2010-08-03T10:48:40Z
dc.date.available2010-08-03T10:48:40Z
dc.date.issued1992-08-31
dc.identifier.citationSite directed mutagenesis of two cysteine residues in the E. coli ogt O6-alkylguanine DNA alkyltransferase protein. 1992, 187 (1):425-31 Biochem. Biophys. Res. Commun.en
dc.identifier.issn0006-291X
dc.identifier.pmid1520330
dc.identifier.doi10.1016/S0006-291X(05)81510-4
dc.identifier.urihttp://hdl.handle.net/10541/108917
dc.description.abstractThe E. coli ogt O6-alkylguanine-DNA alkyltransferase has two cysteine residues positioned identically with respect to cysteines in the E. coli ada O6-alkylguanine-DNA alkyltransferase. In order to assess their function, these residues were each substituted by a glycine to generate altered forms of the ogt protein. Mutagenesis of cysteine-139, located within a 'PCHRV' region of homology, eliminated functional activity confirming that this residue is the methyl-accepting cysteine in the active site of the protein. Substitution of cysteine 102 within the sequence 'LRTIPCG' had little effect on the ogt protein activity demonstrating that this cysteine is not directly involved with the transfer of O6-methylguanine adducts.
dc.language.isoenen
dc.subject.meshAmino Acid Sequence
dc.subject.meshBase Sequence
dc.subject.meshBinding Sites
dc.subject.meshBlotting, Western
dc.subject.meshCysteine
dc.subject.meshDNA, Recombinant
dc.subject.meshEscherichia coli
dc.subject.meshKinetics
dc.subject.meshMethyltransferases
dc.subject.meshMolecular Sequence Data
dc.subject.meshMutagenesis, Site-Directed
dc.subject.meshO(6)-Methylguanine-DNA Methyltransferase
dc.subject.meshRecombinant Fusion Proteins
dc.subject.meshStructure-Activity Relationship
dc.titleSite directed mutagenesis of two cysteine residues in the E. coli ogt O6-alkylguanine DNA alkyltransferase protein.en
dc.typeArticleen
dc.contributor.departmentCRC Department of Chemical Carcinogenesis, Paterson Institute for Cancer Research, Christie Hospital and Holt Radium Institute, Manchester, UK.en
dc.identifier.journalBiochemical and Biophysical Research Communicationsen
html.description.abstractThe E. coli ogt O6-alkylguanine-DNA alkyltransferase has two cysteine residues positioned identically with respect to cysteines in the E. coli ada O6-alkylguanine-DNA alkyltransferase. In order to assess their function, these residues were each substituted by a glycine to generate altered forms of the ogt protein. Mutagenesis of cysteine-139, located within a 'PCHRV' region of homology, eliminated functional activity confirming that this residue is the methyl-accepting cysteine in the active site of the protein. Substitution of cysteine 102 within the sequence 'LRTIPCG' had little effect on the ogt protein activity demonstrating that this cysteine is not directly involved with the transfer of O6-methylguanine adducts.


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