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Titolo:
ONE OF 3 NUCLEAR-LOCALIZATION SIGNALS OF MAIZE ACTIVATOR (AC) TRANSPOSASE OVERLAPS THE DNA-BINDING DOMAIN
Autore:
BOEHM U; HEINLEIN M; BEHRENS U; KUNZE R;
Indirizzi:
UNIV COLOGNE,INST GENET,WEYERTAL 121 D-50931 COLOGNE GERMANY UNIV COLOGNE,INST GENET D-50931 COLOGNE GERMANY
Titolo Testata:
Plant journal
fascicolo: 3, volume: 7, anno: 1995,
pagine: 441 - 451
SICI:
0960-7412(1995)7:3<441:OO3NSO>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ZEA-MAYS-L; ELEMENT-AC; PUTATIVE TRANSPOSASE; PROTEIN LOCALIZATION; TARGETING SEQUENCES; VIRD2 PROTEIN; PLANT NUCLEI; T-DNA; YEAST; PHOSPHOPROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
U. Boehm et al., "ONE OF 3 NUCLEAR-LOCALIZATION SIGNALS OF MAIZE ACTIVATOR (AC) TRANSPOSASE OVERLAPS THE DNA-BINDING DOMAIN", Plant journal, 7(3), 1995, pp. 441-451

Abstract

The nuclear localization sequences (NLSs) of the Ac transposase (TPase) protein have been characterized by indirect immunofluorescence detection of TPase deletion derivatives and TPase/beta-glucuronidase (GUS)fusion proteins in transiently transfected Petunia cells. The TPase contains three NLSs near its amino-terminal end, NLS(44-62), NLS(159-178) and NLS(174-206), each of which is sufficient to redirect GUS to the nucleus. Deletion of the N-terminal 102 TPase residues including NLS(44-62) results in strongly reduced nuclear import of the truncated TPase. NLS(44-62) and NLS(159-178) are bipartite NLSs, whereas the structure of NLS(174-206) does not allow a classification into one of the three major NLS categories. NLS(174-206) overlaps with the basic DNA-binding domain of TPase. A substitution of two amino acids in this segment (His(191)-->Arg and Arg(193)-->His) results in a total loss of DNA-binding activity, but retains reduced NLS activity. Accordingly, the two functions can be separated. In addition, we show that a NLS-deficient 71 kDa TPase derivative is co-imported into the nucleus in the presence of wild-type TPase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 10:19:46