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Titolo:
A highly conserved domain of the maize activator transposase is involved in dimerization
Autore:
Essers, L; Adolphs, RH; Kunze, R;
Indirizzi:
Univ Munich, Inst Genet & Mikrobiol, D-80638 Munich, Germany Univ Munich Munich Germany D-80638 & Mikrobiol, D-80638 Munich, Germany
Titolo Testata:
PLANT CELL
fascicolo: 2, volume: 12, anno: 2000,
pagine: 211 - 223
SICI:
1040-4651(200002)12:2<211:AHCDOT>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
DNA-BINDING DOMAIN; SECONDARY STRUCTURE PREDICTION; ZEA-MAYS-L; ELEMENT-AC; 2-HYBRID SYSTEM; SUBTERMINAL SEQUENCES; PUTATIVE TRANSPOSASE; TN5 TRANSPOSASE; IN-VITRO; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Kunze, R Univ Cologne, Inst Bot, Gyrhofstr 15, D-50931 Cologne, Germany Univ Cologne Gyrhofstr 15 Cologne Germany D-50931 logne, Germany
Citazione:
L. Essers et al., "A highly conserved domain of the maize activator transposase is involved in dimerization", PL CELL, 12(2), 2000, pp. 211-223

Abstract

Previous studies have presented indirect evidence that the transposase of the maize transposable element Activator (TPase) is active as an oligomer and forms inactive macromolecular complexes expressed in large amounts. Here, we have identified and characterized a dimerization domain at the C terminus of the protein. This domain is the most highly conserved region in the transposases of elements belonging to the Activator superfamily PAT elementsuperfamily) and contains a characteristic signature motif. The isolated dimerization domain forms extremely stable dimers in vitro. Interestingly, mutations in five of the six conserved residues of the signature motif do not affect in vitro dimerization, whereas mutations in other, less strictly conserved residues of the signature motif do. Loss of dimerization in vitro correlates with loss of TPase activity in vivo. As revealed by in situ immunofluorescence staining of mutant TPase proteins, the dimerization domain also is involved in forming inactive macromolecular aggregates when overexpressed, and the TPase contains one or more additional interaction functions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 09:26:31