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

Abstract：

:The 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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Harris LC,Potter PM,Margison GP

doi

10.1016/s0006-291x(05)81510-4

subject

Has Abstract

pub_date

1992-08-31 00:00:00

pages

425-31

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)81510-4

journal_volume

187

pub_type

杂志文章

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