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Titolo:
Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch
Autore:
Yang, HJ; Clendenin, WM; Wong, D; Demple, B; Slupska, MM; Chiang, JH; Miller, JH;
Indirizzi:
Univ Calif Los Angeles, Dept Microbiol & Mol Genet, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA Univ Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA Harvard Univ, Sch Publ Hlth, Dept Canc Cell Biol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 ept Canc Cell Biol, Boston, MA 02115 USA
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 3, volume: 29, anno: 2001,
pagine: 743 - 752
SICI:
0305-1048(20010201)29:3<743:EAOAG(>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI MUTY; HUMAN APURINIC ENDONUCLEASE; PURIFIED HUMAN PROTEINS; EXONUCLEASE-III; POLYMERASE-BETA; SYNTHESIS PAST; HUMAN HOMOLOG; ABASIC SITES; LIGASE-I; ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Miller, JH Univ Calif Los Angeles, Dept Microbiol & Mol Genet, 1602 Mol Sci Bldg,405 Hilgard Ave, Los Angeles, CA 90095 USA Univ Calif Los Angeles 1602 Mol Sci Bldg,405 Hilgard Ave Los Angeles CA USA 90095
Citazione:
H.J. Yang et al., "Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch", NUCL ACID R, 29(3), 2001, pp. 743-752

Abstract

Adenine-DNA glycosylase MutY of Escherichia coli catalyzes the cleavage ofadenine when mismatched with 7,8-dihydro-8-oxoguanine (GO), an oxidativelydamaged base. The biological outcome is the prevention of C/G-->A/T transversions. The molecular mechanism of base excision repair (BER) of A/GO in mammals is not well understood. In this study we report stimulation of mammalian adenine-DNA glycosylase activity by apurinic/apyrimidinic (AP) endonuclease using murine homolog of MutY (Myh) and human AP endonuclease (Ape1), which shares 94% amino acid identity with its murine homolog Apex. After removal of adenine by the Myh glycosylase activity, intact AP DNA remains dueto lack of an efficient Myh AP lyase activity. The study of wild-type Ape1and its catalytic mutant H309N demonstrates that Ape1 catalytic activity is required for formation of cleaved AP DNA. It also appears that Ape1 stimulates Myh glycosylase activity by increasing formation of the Myh-DNA complex. This stimulation is independent of the catalytic activity of Ape1, Consequently, Ape1 preserves the Myh preference for A/GO over A/G and improves overall glycosylase efficiency. Our study suggests that protein-protein interactions may occur in vivo to achieve efficient BER of A/GO.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 03:49:52