PMID:6754717

Citation	Demple, B, Jacobsson, A, Olsson, M, Robins, P and Lindahl, T (1982) Repair of alkylated DNA in Escherichia coli. Physical properties of O6-methylguanine-DNA methyltransferase. J. Biol. Chem. 257:13776-80
Abstract	An inducible methyltransferase of Escherichia coli acts on O6-methylguanine in DNA by conveying the methyl group to one of its own cysteine residues. The protein has now been purified to apparent homogeneity from a constitutively expressing strain. The homogeneous methyltransferase exhibits no DNA glycosylase or endonuclease activity on alkylated DNA. Further, the methyltransferase activity is strikingly resistant to heat inactivation under reducing conditions. The protein has Mr = 18,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, while the sedimentation coefficient and Stokes radius of the native enzyme yield Mr = 18,400. The amino acid composition of the purified protein shows 4 to 5 cysteine residues/transferase molecule. The methylated, inactive form of the transferase has an unaltered molecular weight.
Links	PubMed
Keywords	Amino Acids/analysis; DNA Repair; DNA, Bacterial/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Methyltransferases/isolation & purification; Methyltransferases/metabolism; Molecular Weight; O(6)-Methylguanine-DNA Methyltransferase
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECOLI:ADA	involved_in	GO:0080111: DNA demethylation	ECO:0000314: direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
ECOLI:ADA	enables	GO:0003908: methylated-DNA-[protein]-cysteine S-methyltransferase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

References

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