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Titolo:
CHARACTERIZATION OF THE RECOMBINANT MUTY HOMOLOG, AN ADENINE DNA GLYCOSYLASE, FROM YEAST SCHIZOSACCHAROMYCES-POMBE
Autore:
LU AL; FAWCETT WP;
Indirizzi:
UNIV MARYLAND,DEPT BIOCHEM & MOL BIOL BALTIMORE MD 21201
Titolo Testata:
The Journal of biological chemistry
fascicolo: 39, volume: 273, anno: 1998,
pagine: 25098 - 25105
SICI:
0021-9258(1998)273:39<25098:COTRMH>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI MUTY; ENZYME ENDONUCLEASE-III; CATALYTIC MECHANISM; MISMATCH REPAIR; BASE-PAIR; 8-HYDROXYGUANINE 7,8-DIHYDRO-8-OXOGUANINE; MUTAGENIC SUBSTRATE; IONIZING-RADIATION; OXIDATIVE DAMAGE; EXCISION-REPAIR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
A.L. Lu e W.P. Fawcett, "CHARACTERIZATION OF THE RECOMBINANT MUTY HOMOLOG, AN ADENINE DNA GLYCOSYLASE, FROM YEAST SCHIZOSACCHAROMYCES-POMBE", The Journal of biological chemistry, 273(39), 1998, pp. 25098-25105

Abstract

The mutY homolog (SpMYH) gene from a cDNA library of Schizosaccharomyces pombe encodes a protein of 461 amino acids that displays 28 and 31% identity to Escherichia coli MutY and human MutY homolog (MYH), respectively. Expressed SpMYH is able to complement an E. coli mutY mutantto reduce the mutation rate. Similar to E. coli MutY protein, purified recombinant SpMYH expressed in E. coli has adenine DNA glycosylase and apurinic/apyrimidinic lyase activities on A/G- and A/7,8-dihydro-8-oxoguanine (8-oxoG)-containing DNA. However, both enzymes have different salt requirements and slightly different substrate specificities. SpMYH has greater glycosylase activity on 2-aminopurine/G and A/2-aminopurine but weaker activity on A/C than E. coli MutY. Both enzymes alsohave different substrate binding affinity and catalytic parameters. Although SpMYH has great affinity to A/8-oxoG-containing DNA as MutY, the binding affinity to A/G-containing DNA is substantially lower for SpMYH than MutY, SpMYH has similar reactivity to both A/G- and A/8-oxoG-containing DNA; however, MutY cleaves A/G-containing DNA about 3-foldmore efficiently than it does A/8-oxoG-containing DNA. Thus, SpMYH isthe functional eukaryotic MutY homolog responsible for reduction of 8-oxoG mutational effect.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 16:34:50