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Titolo:
MOUSE MTH1 PROTEIN WITH 8-OXO-7,8-DIHYDRO-2'-DEOXYGUANOSINE 5'-TRIPHOSPHATASE ACTIVITY THAT PREVENTS TRANSVERSION MUTATION - CDNA CLONING AND TISSUE DISTRIBUTION
Autore:
KAKUMA T; NISHIDA J; TSUZUKI T; SEKIGUCHI M;
Indirizzi:
KYUSHU UNIV,MED INST BIOREGULAT,DEPT BIOCHEM FUKUOKA 81282 JAPAN KYUSHU UNIV,MED INST BIOREGULAT,DEPT BIOCHEM FUKUOKA 81282 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 43, volume: 270, anno: 1995,
pagine: 25942 - 25948
SICI:
0021-9258(1995)270:43<25942:MMPW85>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; DNA-SYNTHESIS; 8-HYDROXYGUANINE 7,8-DIHYDRO-8-OXOGUANINE; MUTAGENIC SUBSTRATE; NUCLEOTIDE-SEQUENCE; HUMAN-CELLS; MUTT; REPAIR; ENZYME; HYDROLYZES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
T. Kakuma et al., "MOUSE MTH1 PROTEIN WITH 8-OXO-7,8-DIHYDRO-2'-DEOXYGUANOSINE 5'-TRIPHOSPHATASE ACTIVITY THAT PREVENTS TRANSVERSION MUTATION - CDNA CLONING AND TISSUE DISTRIBUTION", The Journal of biological chemistry, 270(43), 1995, pp. 25942-25948

Abstract

8-Oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP) is formed in the nucleotide pool of a cell during normal cellular metabolism, and when it is incorporated into DNA causes mutation. Organisms possess 8-oxo-dGTPase, an enzyme that specifically degrades 8-oxo-dGTP to 8-oxo-dGMP. We isolated cDNA for mouse 8-oxo-dGTPase, using as a probe human MTH1 (Escherichia coli mutT homolog) cDNA. The nucleotide sequence of the cDNA revealed that the mouse MTH1 protein (molecular weight of 17,896) comprises 156 amino acid residues. When the cDNA for mouse 8-oxo-dGTPase was expressed in E. coli mutT(-) mutant cells devoid of their own 8-oxo-dGTPase activity, an 18-kDa protein, which is cross-reactive with an anti-human MTH1 antibody, was formed. In such cells,the level of spontaneous mutation frequency that was elevated reverted to normal. High levels of 8-oxo-dGTPase activity were found in liver, thymus, and large intestine, whereas all other organs examined contained smaller amounts of the enzyme. In embryonic stem cells, an exceedingly high level of the enzyme was present.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 17:08:40