A new gene (alkB) of Escherichia coli that controls sensitivity to methyl methane sulfonate

Kataoka, Hiroko; Yamamoto, Y; Sekiguchi, Mutsuo

doi:10.1128/jb.153.3.1301-1307.1983

Cited by 163 publications

(72 citation statements)

References 25 publications

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“…Two of these genes, ada and aZkB, are cotranscribed from a single promoter and therefore constitute an operon [Kataoka and Sekiguchi, 1985;Kondo et al, 19861. This operon is located at 47 min on the genetic map [Jeggo, 1979;Kataoka et al, 1983;Sedgwick 19821. The third gene is aZkA, which maps at 45 min [Yamamoto et al, 1978;Volkert et al, 19861. A fourth gene, uidB (95 min), is also part of the adaptive response, but its role in survival or mutagenesis has not been established [Volkert et al, 19861.…”

Section: Genetics Of the Adaptive Responsementioning

confidence: 99%

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Adaptive response of escherichia coli to alkylation damage

Volkert

1988

Environ and Mol Mutagen

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Treatment of cells with low levels of alkylating agents for extended periods of time causes them to become resistant to the lethal and mutagenic effects of subsequent high-level challenge treatments with alkylating agents. This increased resistance has been called the adaptive response to alkylation damage and results from the induction of an alkylation-specific DNA repair response. The adaptive response is most efficiently induced by methylating agents and is most effective against the lethal and mutagenic effects of methylation damage to DNA. Four genes have been identified as components of this response, ada, alkA, alkB and aidB. The functions of two of these genes are known. AlkA protein functions as a glycosylase that repairs N3-meA, N3-meG, O2-meT, and O2-meC residues in DNA, and Ada protein functions as an alkyltransferase that removes alkyl groups from O6-meG, O4-meT residues as well as methylphosphotriesters. After it interacts with methylated DNA, Ada protein functions as a positive regulatory element that controls the expression of the adaptive response by stimulating the expression of the ada-alkB operon, and the alkA and aidB genes.

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Section: Genetics Of the Adaptive Responsementioning

confidence: 99%

“…Mutations in uda, alkA, and alkB cause increased sensitivity to either the lethal or the mutagenic (or both) effects of methylation damage [Jeggo, 1979;Kataoka et al, 1983;Yamamoto et al, 19781. The sensitivities of ada and alkA mutants to alkylation damage are ascribed to their inability to repair specific lesions.…”

Section: Genetics Of the Adaptive Responsementioning

confidence: 99%

Adaptive response of escherichia coli to alkylation damage

Volkert

1988

Environ and Mol Mutagen

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“…The Escherichia coli alkB gene was discovered more than 20 years ago (Kataoka et al, 1983). An indication on the nature of the substrates came from the observation that AlkB specifically reactivated methylated single-stranded DNA bacteriophages, where 1-meA and 3-meC are major cytotoxic lesions (Dinglay et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Human ABH3 structure and key residues for oxidative demethylation to reverse DNA/RNA damage

Sundheim

Vågbø²,

Bjørås

et al. 2006

EMBO J

161

226

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Methylating agents are ubiquitous in the environment, and central in cancer therapy. The 1-methyladenine and 3-methylcytosine lesions in DNA/RNA contribute to the cytotoxicity of such agents. These lesions are directly reversed by ABH3 (hABH3) in humans and AlkB in Escherichia coli. Here, we report the structure of the hABH3 catalytic core in complex with iron and 2-oxoglutarate (2OG) at 1.5 Å resolution and analyse key sitedirected mutants. The hABH3 structure reveals the b-strand jelly-roll fold that coordinates a catalytically active iron centre by a conserved His 1 -X-Asp/Glu-X n -His 2 motif. This experimentally establishes hABH3 as a structural member of the Fe(II)/2OG-dependent dioxygenase superfamily, which couples substrate oxidation to conversion of 2OG into succinate and CO 2 . A positively charged DNA/RNA binding groove indicates a distinct nucleic acid binding conformation different from that predicted in the AlkB structure with three nucleotides. These results uncover previously unassigned key catalytic residues, identify a flexible hairpin involved in nucleotide flipping and ss/ds-DNA discrimination, and reveal self-hydroxylation of an active site leucine that may protect against uncoupled generation of dangerous oxygen radicals.

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“…When Ada is methylated at position 69 (reAda), it can bind to specific DNA sequences in the promoter region of the adaptive response genes, and activate their transcription (Nakabeppu and Sekiguchi, 1986;Teo et al, 1986). Four genes (ada, aidB, alkA and alkB) have been identified so far as components of this regulon (Jeggo, 1979;Karran et al, 1982;Kataoka et al, 1983;Volkert and Nguyen, 1984). The alkA gene encodes a glycosylase responsible for the excision of methylated bases from DNA.…”

Section: Introductionmentioning

confidence: 99%

RNA polymerase alpha subunit binding site in positively controlled promoters: a new model for RNA polymerase-promoter interaction and transcriptional activation in the Escherichia coli ada and aidB genes.

Landini

Volkert

1995

The EMBO Journal

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The ada and aidB genes are part of the adaptive response to DNA methylation damage in Escherichia coli. Transcription of the ada and the aidB genes is triggered by binding of the methylated Ada protein (meAda) to a specific sequence located 40–60 base pairs upstream of the transcriptional start, which is internal to an A/T‐rich region. In this report we demonstrate that the Ada binding site is also a binding site for RNA polymerase. RNA polymerase is able to bind the −40 to −60 region of the ada and the aidB promoters in the absence of meAda, and its binding is mediated by the alpha subunit. This region resembles the UP element of the rrnB P1 promoter in location, sequence and mechanism of interaction with RNA polymerase. We discuss the function of UP‐like elements in positively controlled promoters and provide evidence that Ada does not act by enhancing RNA polymerase binding affinity to the promoter region. Instead, Ada stimulates transcription by modifying the nature of the RNA polymerase‐promoter interaction, allowing RNA polymerase to recognize the core promoter −35 and −10 elements in addition to the UP‐like element.

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A new gene (alkB) of Escherichia coli that controls sensitivity to methyl methane sulfonate

Cited by 163 publications

References 25 publications

Adaptive response of escherichia coli to alkylation damage

Adaptive response of escherichia coli to alkylation damage

Human ABH3 structure and key residues for oxidative demethylation to reverse DNA/RNA damage

RNA polymerase alpha subunit binding site in positively controlled promoters: a new model for RNA polymerase-promoter interaction and transcriptional activation in the Escherichia coli ada and aidB genes.

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