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Titolo:
INHIBITION OF CELL-PROLIFERATION IN SACCHAROMYCES-CEREVISIAE BY EXPRESSION OF HUMAN NAD-RIBOSYLTRANSFERASE REQUIRES THE DNA-BINDING DOMAIN (ZINC FINGERS)( ADP)
Autore:
KAISER P; AUER B; SCHWEIGER M;
Indirizzi:
UNIV INNSBRUCK,INST BIOCHEM,PETER MAYR STR 1A A-6020 INNSBRUCK AUSTRIA
Titolo Testata:
MGG. Molecular & general genetics
fascicolo: 2, volume: 232, anno: 1992,
pagine: 231 - 239
SICI:
0026-8925(1992)232:2<231:IOCISB>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN POLY(ADP-RIBOSE) POLYMERASE; DIVERGENT GAL1-GAL10 PROMOTER; ESCHERICHIA-COLI; YEAST; CDNA; GENE; SYNTHETASE; SEQUENCES; CLONING; VECTORS;
Keywords:
HUMAN ADP-RIBOSYLTRANSFERASE; YEAST EXPRESSION; DNA BINDING DOMAIN; ZINC FINGER;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
P. Kaiser et al., "INHIBITION OF CELL-PROLIFERATION IN SACCHAROMYCES-CEREVISIAE BY EXPRESSION OF HUMAN NAD-RIBOSYLTRANSFERASE REQUIRES THE DNA-BINDING DOMAIN (ZINC FINGERS)( ADP)", MGG. Molecular & general genetics, 232(2), 1992, pp. 231-239

Abstract

Constitutive expression of human nuclear NAD+: protein ADP-ribosyltransferase (polymerizing) [pADPRT; poly(ADP-ribose)polymerase; EC 2.4.2.30] as an active enzyme in Saccharomyces cerevisiae, under the controlof the alcohol dehydrogenase promoter, was only possible with simultaneous inhibition of ADP-ribosylation by 3-methoxybenzamide. Induction of fully active pADPRT from the inducible galactose epimerase promoterresulted in inhibition of cell division and morphological changes reminiscent of cell cycle mutants. Expression of a pADPRT cDNA truncated at its 5' end had no influence on cell proliferation at all. Obviouslythe amino-terminal part of the DNA binding domain containing the first "zinc finger", which is essential for inducibility of pADPRT activity by DNA breaks, is also required for inhibition of cell growth on expression in yeast. Full-length as well as truncated pADPRT molecules were directed to the cell nucleus where the fully active enzyme producedlarge amounts of poly(ADP-ribose) by automodification. Since pADPRT turned out to be the only target for ADP-ribosylation in these cells, elevated levels of poly(ADP-ribose) were the most likely cause of inhibition of cell division, presumably resulting from interaction with chromosomal proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/05/20 alle ore 01:20:10