A second DNA methyltransferase repair enzyme in Escherichia coli.
about
Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16Mismatch repair proteins collaborate with methyltransferases in the repair of O(6)-methylguaninePrimary sequence and biological functions of a Saccharomyces cerevisiae O6-methylguanine/O4-methylthymine DNA repair methyltransferase gene.The Saccharomyces cerevisiae MGT1 DNA repair methyltransferase gene: its promoter and entire coding sequence, regulation and in vivo biological functions.Cloning a eukaryotic DNA glycosylase repair gene by the suppression of a DNA repair defect in Escherichia coli.Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to the AlkA glycosylase of E. coli and is induced in response to DNA alkylation damage.Increased spontaneous mutation and alkylation sensitivity of Escherichia coli strains lacking the ogt O6-methylguanine DNA repair methyltransferaseThe solution structure of the methylated form of the N-terminal 16-kDa domain of Escherichia coli Ada protein.Systems based mapping demonstrates that recovery from alkylation damage requires DNA repair, RNA processing, and translation associated networks.Purification to homogeneity and partial amino acid sequence of a fragment which includes the methyl acceptor site of the human DNA repair protein for O6-methylguanineChemical biology of mutagenesis and DNA repair: cellular responses to DNA alkylationBacillus subtilis gene coding for constitutive O6-methylguanine-DNA alkyltransferase.Construction and characterization of mutants of Salmonella typhimurium deficient in DNA repair of O6-methylguanineSuppression of Escherichia coli alkB mutants by Saccharomyces cerevisiae genes.The Escherichia coli AlkB protein protects human cells against alkylation-induced toxicity.New method for gene disruption in Salmonella typhimurium: construction and characterization of an ada-deletion derivative of Salmonella typhimurium TA1535.Mutagenic frequencies of site-specifically located O6-methylguanine in wild-type Escherichia coli and in a strain deficient in ada-methyltransferase.Cloning and characterization of the Salmonella typhimurium ada gene, which encodes O6-methylguanine-DNA methyltransferaseCharacterization of the major DNA repair methyltransferase activity in unadapted Escherichia coli and identification of a similar activity in Salmonella typhimurium.Construction of an Escherichia coli K-12 ada deletion by gene replacement in a recD strain reveals a second methyltransferase that repairs alkylated DNAAlteration of the carboxyl-terminal domain of Ada protein influences its inducibility, specificity, and strength as a transcriptional activatorExpression of the ogt gene in wild-type and ada mutants of E. coli.A molecular bar-coded DNA repair resource for pooled toxicogenomic screens.The influence of DNA repair by Ogt alkyltransferase on the distribution of alkylnitrosourea-induced mutations in Escherichia coli.
P2860
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P2860
A second DNA methyltransferase repair enzyme in Escherichia coli.
description
1988 nî lūn-bûn
@nan
1988 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
A second DNA methyltransferase repair enzyme in Escherichia coli.
@ast
A second DNA methyltransferase repair enzyme in Escherichia coli.
@en
A second DNA methyltransferase repair enzyme in Escherichia coli.
@nl
type
label
A second DNA methyltransferase repair enzyme in Escherichia coli.
@ast
A second DNA methyltransferase repair enzyme in Escherichia coli.
@en
A second DNA methyltransferase repair enzyme in Escherichia coli.
@nl
prefLabel
A second DNA methyltransferase repair enzyme in Escherichia coli.
@ast
A second DNA methyltransferase repair enzyme in Escherichia coli.
@en
A second DNA methyltransferase repair enzyme in Escherichia coli.
@nl
P2093
P2860
P356
P1476
A second DNA methyltransferase repair enzyme in Escherichia coli.
@en
P2093
P2860
P304
P356
10.1073/PNAS.85.9.3039
P407
P577
1988-05-01T00:00:00Z