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Titolo:
The C-terminal domain of MutY glycosylase determines the 7,8-dihydro-8-oxo-guanine specificity and is crucial for mutation avoidance
Autore:
Li, XH; Wright, PM; Lu, AL;
Indirizzi:
Univ Maryland, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 & Mol Biol, Baltimore, MD 21201 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 12, volume: 275, anno: 2000,
pagine: 8448 - 8455
SICI:
0021-9258(20000324)275:12<8448:TCDOMG>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI MUTY; DNA-REPAIR ENZYME; NUCLEOTIDE EXCISION-REPAIR; G-A MISPAIRS; MISMATCH REPAIR; ENDONUCLEASE-III; SUBSTRATE-SPECIFICITY; CATALYTIC MECHANISM; DAMAGED DNA; GENE-PRODUCT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Lu, AL Univ Maryland, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 Biol, Baltimore, MD 21201 USA
Citazione:
X.H. Li et al., "The C-terminal domain of MutY glycosylase determines the 7,8-dihydro-8-oxo-guanine specificity and is crucial for mutation avoidance", J BIOL CHEM, 275(12), 2000, pp. 8448-8455

Abstract

Escherichia coli MutY is an adenine DNA glycosylase active on DNA substrates containing A/G, A/8-oxoG, or A/C mismatches and also has a weak guanine glycosylase activity on G/8-oxoG-containing DNA. The N-terminal domain of MutY, residues 1-226, has been shown to retain catalytic activity. Substratebinding, glycosylase, and Schiff base intermediate formation activities ofthe truncated and intact MutY were compared. MutY has high binding affinity with 8-oxoG when mispaired with A, G, T, C, or inosine, The truncated protein has more than 18-fold Lower affinities for binding various 8-oxoG-containing mismatches when compared with intact MutY. MutY catalytic activity toward A/8-oxoG-containing DNA is much faster than that on A/G-containing DNA whereas deletion of the C-terminal domain reduces its catalytic preference for A/8-oxoG-DNA over A/G-DNA. MutY exerts more inhibition on the catalytic activity of MutM (Fpg) protein than does truncated MutY, The tight binding of MutY with GO mispaired with T, G, and apurinic/apyrimidinic sites maybe involved in the regulation of MutM activity. An E. colt mutY strain that produces an N-terminal 249-residue truncated MutY confers a mutator phenotype, These findings strongly suggest that the C-terminal domain of MutY determines the 8-oxoG specificity and is crucial for mutation avoidance by oxidative damage.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/10/20 alle ore 12:04:53