Mutator specificity of Escherichia coli alkB117 allele

• Autorzy: Nieminuszczy J. , Janion C. , Grzesiuk E.
• Języki publikacji: EN

Abstrakty

EN

The Escherichia coli AlkB protein encoded by alkB gene was recently found to repair cytotoxic DNA lesions 1-methyladenine (1-meA) and 3-methylcytosine (3-meC) by using a novel iron-catalysed oxidative demethylation mechanism that protects the cell from the toxic effects of methylating agents. Mutation in alkB results in increased sensitivity to MMS and elevated level of MMS-induced mutations. The aim of this study was to analyse the mutational specificity of alkB117 in a system developed by J.H. Miller involving two sets of E. coli lacZ mutants, CC101-106 allowing the identification of base pair substitutions, and CC107-CC111 indicating frameshift mutations. Of the six possible base substitutions, the presence of alkB117 allele led to an increased level of GC→AT transitions and GC→TA and AT→TA transversions. After MMS treatment the level of GC→AT transitions increased the most, 22-fold. Among frameshift mutations, the most numerous were -2CG, -1G, and -1A deletions and +1G insertion. MMS treatment appreciably increased all of the above types of frameshifts, with additional appearance of the +1A insertion.

Słowa kluczowe

EN

1-methyladenine; mutational specificity; methyl methanesulphonate; 3-methylcytosine; Escherichia coli; alkB gene; allele; AlkB protein

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2006
• Tom: 53
• Numer: 2
• Opis fizyczny: p.425-428,fig.,ref.

Twórcy

autor

Nieminuszczy J.

• Polish Academy of Sciences, Warsaw, Poland

autor

Janion C.

autor

Grzesiuk E.

Bibliografia

• Begley TJ, Samson LD (2003) Trends Biochem Sci 28: 2–5.
• Borden A, O’Grady PI, Vandewiele D, Fernandez de Henestrosa AR, Lawrence CW, Woodgate R (2002) J Bacteriol 184: 2674–2681.
• Cupples CG, Miller JH (1989) Proc Natl Acad Sci USA 86: 5345–5349.
• Cupples CG, Cabrera M, Cruz C, Miller JH (1990) Genetics 125: 275–280.
• Delaney JC, Essigmann JM (2004) Proc Natl Acad Sci USA 101: 14051–14056.
• Dinglay S, Trewick SC, Lindahl T, Sedgwick B (2000) Genes Develop 14: 2097–2105.
• Falnes PO, Rognes T (2003) Res Microbiol 154: 531–538.
• Fuchs RP, Fujii S, Wagner J (2004) Adv Prot Chem 69: 229–264.
• Grzesiuk E (1998) Acta Biochim Polon 45: 523–533.
• Grzesiuk E, Janion C (1994) Mol Gen Genet 245: 486–492.
• Kataoka H, Yamamoto Y, Sekiguchi M (1983) J Bacteriol 153: 1301–1307.
• Miller JH (1972) Experiments in Molecular Genetics, pp. 215–217, Cold Spring Harbor Laboratory, New York.
• Nieminuszczy J, Sikora A, Wrzesinski M, Janion C, Grzesiuk E (2006) DNA Repair 5: 181–188.
• Samson L, Cairns J (1977) Nature 267: 281–283.
• Sedgwick B (1992) Cancer Res 52: 3693–3697.
• Sedgwick B (2004) Nat Rev Mol Cell Biol 5: 148–157.
• Taverna P, Sedgwick B (1996) J Bacteriol 178: 5105–5111.
• Trewick SC, Henshaw TF, Hausinger RP, Lindahl T, Sedgwick B (2002) Nature 419: 174–178.
• Vogel HJ, Bonner DM (1956) J Biol Chem 218: 97–106.