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Titolo:
SIGNIFICANCE OF THE CONSERVED AMINO-ACID-SEQUENCE FOR HUMAN MTH1 PROTEIN WITH ANTIMUTATOR ACTIVITY
Autore:
CAI JP; KAWATE H; IHARA K; YAKUSHIJI H; NAKABEPPU Y; TSUZUKI T; SEKIGUCHI M;
Indirizzi:
FUKUOKA DENT COLL,DEPT BIOL FUKUOKA 81401 JAPAN KYUSHU UNIV,MED INST BIOREGULAT,DEPT BIOCHEM FUKUOKA 81282 JAPAN
Titolo Testata:
Nucleic acids research
fascicolo: 6, volume: 25, anno: 1997,
pagine: 1170 - 1176
SICI:
0305-1048(1997)25:6<1170:SOTCAF>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI MUTT; OXIDATIVE DNA DAMAGE; C-G TRANSVERSION; 8-HYDROXYGUANINE 7,8-DIHYDRO-8-OXOGUANINE; MUTAGENIC SUBSTRATE; HUMAN-CELLS; A-T; HOMOLOG; 8-OXO-DGTPASE; MUTATIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
J.P. Cai et al., "SIGNIFICANCE OF THE CONSERVED AMINO-ACID-SEQUENCE FOR HUMAN MTH1 PROTEIN WITH ANTIMUTATOR ACTIVITY", Nucleic acids research, 25(6), 1997, pp. 1170-1176

Abstract

8-Oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP) is produced during normal cellular metabolism, and incorporation into DNA causes transversion mutation, Organisms possess an enzyme, 8-oxo-dGTPase, which catalyzes the hydrolysis of 8-oxo-dGTP to the corresponding nucleoside monophosphate, thereby preventing the occurrence of mutation, There are highly conserved amino acid sequences in prokaryotic and eukaryotic proteins containing this and related enzyme activities, To elucidate the significance of the conserved sequence, amino acid substitutions were introduced by site-directed mutagenesis of the cloned cDNA for human 8-oxo-dGTPase, and the activity and stability of mutant forms of the enzyme were examined, When lysine-38 was replaced by otheramino acids, air of the mutants isolated carried the 8-oxo-dGTPase-negative phenotype, 8-Oxo-dGTPase-positive revertants, isolated from oneof the negative mutants, carried the codon for lysine, Using the sameprocedure, the analysis was extended to other residues within the conserved sequence, At the glutamic acid-43, arginine-51 and glutamic acid-52 sites, all the positive revertants isolated carried codons for amino acids identical to those of the wild type protein, We propose thatLys-38, Glu-43, Arg-51 and Glu-52 residues in the conserved region are essential to exert 8-oxo-dGTPase activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/08/20 alle ore 00:50:30