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Titolo:
Differential DNA recognition and glycosylase activity of the native human MutY homolog (hMYH) and recombinant hMYH expressed in bacteria
Autore:
Gu, YS; Lu, AL;
Indirizzi:
Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 & Mol Biol, Baltimore, MD 21201 USA
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 12, volume: 29, anno: 2001,
pagine: 2666 - 2674
SICI:
0305-1048(20010615)29:12<2666:DDRAGA>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI MUTY; MISMATCH REPAIR PROTEIN; SACCHAROMYCES-CEREVISIAE; MAMMALIAN HOMOLOG; HUMAN-CELLS; OGG1 GENE; CLONING; DAMAGE; 8-OXOGUANINE; MITOCHONDRIA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Lu, AL Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 Biol, Baltimore, MD 21201 USA
Citazione:
Y.S. Gu e A.L. Lu, "Differential DNA recognition and glycosylase activity of the native human MutY homolog (hMYH) and recombinant hMYH expressed in bacteria", NUCL ACID R, 29(12), 2001, pp. 2666-2674

Abstract

Human MutY homolog (hMYH), an adenine DNA glycosylase, can effectively remove misincorporated adenines opposite template G or 8-oxoG bases, thereby preventing G:C-->T:A transversions. Human cell extracts possess the adenine DNA glycosylase activity of hMYH and can form protein-DNA complexes with both A/G and A/8-oxoG mismatches, hMYH in cell extracts was shown to be the primary binding protein for A/G- and A/8-oxoG-containing DNA substrates by UV cross-linking. However, recombinant hMYH expressed in bacteria has much weaker glycosylase and substrate-binding activities towards A/G mismatches than native hMYH. Moreover, the protein-DNA complex of bacterially expressedhMYH migrates much faster than that of native hMYH in a non-denaturing polyacrylamide gel. Dephosphorylation of native hMYH reduces the glycosylase activity on A/G more extensively than on A/8-oxoG mismatches but does not alter the gel mobility of the protein-DNA complex. Our results suggest that hMYH in human cell extracts may be associated with other factors in the protein-DNA complex to account for its slower mobility in the gel. hMYH and apurinic/apyrimidinic endonuclease (hAPE1) co-migrate with the protein-DNA complex formed by the extracts and A/8-oxoG-containing DNA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 13:29:36