Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Molecular cloning and functional analysis of the MutY homolog of Deinococcus radiodurans
Autore:
Li, XH; 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:
JOURNAL OF BACTERIOLOGY
fascicolo: 21, volume: 183, anno: 2001,
pagine: 6151 - 6158
SICI:
0021-9193(200111)183:21<6151:MCAFAO>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI MUTY; C-TERMINAL DOMAIN; DNA-REPAIR ENZYME; SCHIFF-BASE INTERMEDIATE; G-A MISPAIRS; ADENINE GLYCOSYLASE; SUBSTRATE-SPECIFICITY; CATALYTIC MECHANISM; IONIZING-RADIATION; EXCISION-REPAIR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Lu, AL Univ Maryland, Sch Med, Dept Biochem & Mol Biol, 108 N Greene St, Baltimore, MD 21201 USA Univ Maryland 108 N Greene St Baltimore MD USA 21201, MD 21201 USA
Citazione:
X.H. Li e A.L. Lu, "Molecular cloning and functional analysis of the MutY homolog of Deinococcus radiodurans", J BACT, 183(21), 2001, pp. 6151-6158

Abstract

The mutY homolog gene (mutY(Dr)) from Deinococcus radiodurans encodes a 39.4-kDa protein consisting of 363 amino acids that displays 35% identity to the Escherichia coli MutY (MutY(Ec)) protein. Expressed MutY(Dr) is able tocomplement E. coli mutY mutants but not mutM mutants to reduce the mutation frequency. The glycosylase and binding activities of MutY(Dr) with an A/G-containing substrate are more sensitive to high salt and EDTA concentrations than the activities with an A/7,8-dihydro-S-oxoguanine (GO)-containing substrate are. Like the MutY(Ec) protein, purified recombinant MutY(Dr) expressed in E. coli has adenine glycosylase activity with A/G, A/C, and A/GO mismatches and weak guanine glycosylase activity with a G/GO mismatch. However, MutY(Dr) exhibits limited apurinic/apyrimidinic lyase activity and can form only weak covalent protein-DNA complexes in the presence of sodium borohydride. This may be due to an arginine residue that is present in MutY(Dr) at the position corresponding to the position of MutY(Ec) Lys142, which forms the Schiff base with DNA. The kinetic parameters of MutY(Dr) are similar to those of MutY(Ec). Although MutY(Dr) has similar substrate specificity and a binding preference for an A/GO mismatch over an A/G mismatch, as MutY(Ec) does, the binding affinities for both mismatches are slightly lower for MutY(Dr) than for MutY(Ec). Thus, MutY(Dr) can protect the cell from GOmutational effects caused by ionizing radiation and oxidative stress.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 02:57:41