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Titolo:
CHARACTERIZATION OF A MAMMALIAN HOMOLOG OF THE ESCHERICHIA-COLI MUTY MISMATCH REPAIR PROTEIN
Autore:
MCGOLDRICK JP; YEH YC; SOLOMON M; ESSIGMANN JM; LU AL;
Indirizzi:
UNIV MARYLAND,SCH MED,DEPT BIOL CHEM BALTIMORE MD 21201 UNIV MARYLAND,SCH MED,DEPT BIOL CHEM BALTIMORE MD 21201 MIT,DEPT CHEM CAMBRIDGE MA 02139
Titolo Testata:
Molecular and cellular biology
fascicolo: 2, volume: 15, anno: 1995,
pagine: 989 - 996
SICI:
0270-7306(1995)15:2<989:COAMHO>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
G-A MISPAIRS; SACCHAROMYCES-CEREVISIAE; NUCLEOTIDE-SEQUENCE; NUCLEAR EXTRACTS; HUMAN-CELLS; BASE-PAIR; DNA GLYCOSYLASE; 8-HYDROXYGUANINE 7,8-DIHYDRO-8-OXOGUANINE; MUTAGENIC SUBSTRATE; COLORECTAL-CANCER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
75
Recensione:
Indirizzi per estratti:
Citazione:
J.P. Mcgoldrick et al., "CHARACTERIZATION OF A MAMMALIAN HOMOLOG OF THE ESCHERICHIA-COLI MUTY MISMATCH REPAIR PROTEIN", Molecular and cellular biology, 15(2), 1995, pp. 989-996

Abstract

A protein homologous to the Escherichia coli MutY protein, referred to as MYH, has been identified in nuclear extracts of calf thymus and human HeLa cells. Western blot (immunoblot) analysis using polyclonal antibodies to the E. coil MutY protein detected a protein of 65 kDa in both extracts. Partial purification of MYH from calf thymus cells revealed a 65-kDa protein as web as a functional but apparently degraded form of 36 kDa, as determined by glycerol gradient centrifugation and immunoblotting with anti-MutY antibodies. Calf MYH is a DNA glycosylasethat specifically removes mispaired adenines from A/G, A/7,8-dihydro-8-oxodeoxyguanine (8-oxoG or GO), and A/C mismatches (mismatches indicated by slashes). A nicking activity that is either associated with orcopurified with MYH was also detected. Nicking was observed at the first phosphodiester bond 3' to the apurinic or apyrimidinic (AP) site generated by the glycosylase activity. The nicking activity on A/C mismatches was 30-fold lower and the activity on A/GO mismatches was twofold lower than that on A/G mismatches. No nicking activity was detectedon substrates containing other selected mismatches or homoduplexes. Nicking activity on DNA containing A/G mismatches was inhibited in the presence of anti-MutY antibodies or upon treatment with potassium ferricyanide, which oxidizes iron-sulfur clusters. Gel shift analysis showed specific binding complex formation with A/G and A/GO substrates, but not with A/A, C.GO, and C.G substrates. Binding is sevenfold greateron A/GO substrates than on A/G substrates. The eukaryotic MYH may be involved in the repair of both replication errors and oxidative damageto DNA, the same functions as those of the E. coli MutY protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 20:18:35