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Titolo:
BIOCHEMICAL AND PHYSICOCHEMICAL CHARACTERIZATION OF NORMAL AND VARIANT FORMS OF HUMAN MTH1 PROTEIN WITH ANTIMUTAGENIC ACTIVITY
Autore:
YAKUSHIJI H; MARABOEUF F; TAKAHASHI M; DENG ZS; KAWABATA S; NAKABEPPU Y; SEKIGUCHI M;
Indirizzi:
FUKUOKA DENT COLL,DEPT BIOL FUKUOKA 81401 JAPAN FUKUOKA DENT COLL,DEPT BIOL FUKUOKA 81401 JAPAN KYUSHU UNIV,FAC SCI,DEPT BIOL FUKUOKA 81281 JAPAN INST CURIE,CNRS,UMR 216 F-91405 ORSAY FRANCE KYUSHU UNIV,MED INST BIOREGULAT,DEPT BIOCHEM FUKUOKA 81282 JAPAN
Titolo Testata:
Mutation research. DNA repair
fascicolo: 3, volume: 384, anno: 1997,
pagine: 181 - 194
SICI:
0921-8777(1997)384:3<181:BAPCON>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI MUTT; GENERATES G.C->T.A TRANSVERSIONS; C-G TRANSVERSION; DNA-SYNTHESIS; 8-HYDROXYGUANINE 7,8-DIHYDRO-8-OXOGUANINE; FOLDING THERMODYNAMICS; MUTAGENIC SUBSTRATE; RNA-POLYMERASE; MUTATOR LOCUS; CLONED GENES;
Keywords:
HUMAN MTH1 PROTEIN; MUTT HOMOLOG; 8-OXO-DGTPASE; THERMOSTABILITY; PREDICTION OF THE SECONDARY STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
61
Recensione:
Indirizzi per estratti:
Citazione:
H. Yakushiji et al., "BIOCHEMICAL AND PHYSICOCHEMICAL CHARACTERIZATION OF NORMAL AND VARIANT FORMS OF HUMAN MTH1 PROTEIN WITH ANTIMUTAGENIC ACTIVITY", Mutation research. DNA repair, 384(3), 1997, pp. 181-194

Abstract

8-Oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP) is produced during cellular metabolism, and its misincorporation into DNA causes mutation. Human cells possess an enzyme that hydrolyzes 8-oxo-dGTP to the corresponding nucleoside monophosphate, thereby preventing misincorporation of 8-oxo-7,8-dihydroguanine into DNA. Sequence analyses of the MTH1 gene, encoding the 8-oxo-7, 8-dihydro-2'-deoxyguanosine5'-triphosphatase (8-oxo-dGTPase) protein in human cell lines revealed that a G to A base substitution frequently occurs at codon 83, whichcauses a change of valine to methionine in the MTH1 protein [Wu, C. et al., Biochem. Biophys. Res. Commun. 214 (1995) 1239-1245]. Here we isolated cDNAs for the two types of MTH1 protein and expressed them in Escherichia coli mutT(-) cells, devoid of their own 8-oxo-dGTPase activity. The two forms of proteins were purified to physical homogeneity,and amino acid analyses confirmed that the variant protein, Met(83)-MTH1, indeed carries the corresponding amino acid substitution. Met(83)-MTH1, but not normal type Val(83)-MTH1, was separated into two peaks in hydrophobic interacting chromatography. 8-Oxo-dGTPase activity of Met(83)-MTH1 is more thermolabile than that of Val(83)-MTH1. Circular dichroism (CD) and fluorescence spectroscopic analyses confirmed this conclusion. CD further indicated that Met(83)-MTH1 has a higher alpha-helix content. Substitution of valine for methionine at the residue 83 of MTH1 protein appears to lead to alteration in the secondary structure which renders the protein more labile than the normal type protein. (C) 1997 Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 19:54:17