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Titolo:
IN-VIVO AGGREGATION OF MAIZE ACTIVATOR (AC) TRANSPOSASE IN NUCLEI OF MAIZE ENDOSPERM AND PETUNIA PROTOPLASTS
Autore:
HEINLEIN M; BRATTIG T; 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: 5, volume: 5, anno: 1994,
pagine: 705 - 714
SICI:
0960-7412(1994)5:5<705:IAOMA(>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ZEA-MAYS-L; ELEMENT-AC; RECA PROTEIN; ARABIDOPSIS-THALIANA; PUTATIVE TRANSPOSASE; EXCISION FREQUENCY; TRANSGENIC TOBACCO; ESCHERICHIA-COLI; TRANSCRIPTION; LOCALIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
M. Heinlein et al., "IN-VIVO AGGREGATION OF MAIZE ACTIVATOR (AC) TRANSPOSASE IN NUCLEI OF MAIZE ENDOSPERM AND PETUNIA PROTOPLASTS", Plant journal, 5(5), 1994, pp. 705-714

Abstract

The transposase (TPase) of the maize transposon Activator (Ac) accumulates in the nuclei of maize endosperm and transfected Petunia protoplasts, where it aggregates into rod-like structures about 2 mu m in length. In petunia protoplasts the amount of TPase aggregates increases with the strength of the promoter fused to the Ac-coding region. The excision frequency of a Ds element, however, does not increase proportionally. The data suggest that the aggregated TPase is not responsible for the mobilization of the Ds element, but rather is a transpositionally inactive form of the protein. In contrast to the full-length TPase,a functional, N-terminally truncated TPase derivative is inefficiently transported into the nucleus at high expression levels and aggregates predominantly in the cytoplasm. Accordingly, the N-terminus of the TPase is involved in nuclear localization and/or aggregation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 06:19:31