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Titolo:
The nuclear receptor Ftz-F1 and homeodomain protein Ftz interact through evolutionarily conserved protein domains
Autore:
Yussa, M; Lohr, U; Su, K; Pick, L;
Indirizzi:
Mt Sinai Sch Med, Dept Biochem & Mol Biol, New York, NY 10029 USA Mt SinaiSch Med New York NY USA 10029 & Mol Biol, New York, NY 10029 USA
Titolo Testata:
MECHANISMS OF DEVELOPMENT
fascicolo: 1-2, volume: 107, anno: 2001,
pagine: 39 - 53
SICI:
0925-4773(200109)107:1-2<39:TNRFAH>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
STEROIDOGENIC FACTOR-I; FUSHI-TARAZU GENE; DNA-BINDING SPECIFICITY; HORMONE-RECEPTOR; TRANSCRIPTIONAL ACTIVATION; DROSOPHILA-MELANOGASTER; GLUCOCORTICOID RECEPTOR; SYNERGISTIC ACTIVATION; TRANSACTIVATION DOMAIN; FUNCTIONAL DISSECTION;
Keywords:
transcription regulation; nuclear hormone receptor; homeodomain; Ftz; SF-1;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
103
Recensione:
Indirizzi per estratti:
Indirizzo: Pick, L Mt Sinai Sch Med, Dept Biochem & Mol Biol, 1 Gustave L Levy Pl, New York, NY 10029 USA Mt Sinai Sch Med 1 Gustave L Levy Pl New York NY USA 10029 029 USA
Citazione:
M. Yussa et al., "The nuclear receptor Ftz-F1 and homeodomain protein Ftz interact through evolutionarily conserved protein domains", MECH DEVEL, 107(1-2), 2001, pp. 39-53

Abstract

The Drosophila homeodomain protein Fushi Tarazu (Ftz) and its partner, theorphan receptor Ftz-F1. are members of two distinct families of DNA binding transcriptional regulators. Ftz and Ftz-F1 form a novel partnership in vivo as a Hox/orphan receptor heterodimer. Here we show that the murine Ftz-F1 ortholog SF-1 functionally substitutes for Ftz-F1 in vivo. rescuing the defects of ftz-f1 mutants. This finding identified evolutionarily conserved domains of Ftz-F1 as critical for activity of this receptor in vivo. These domains function. at least in part. by mediating direct protein interactions with Ftz. The Ftz-F1 DNA binding domain interacts strongly with Ftz and dramatically facilitates the binding of Ftz to target DNA. This interaction is augmented by a second interaction between the AF-2 domain of Ftz-F1 and the N-terminus of Ftz via an LRALL sequence in Ftz that is reminiscent of LXXLL motifs in nuclear receptor coactivators. We propose that Ftz-F1 servesas a cofactor for Ftz by facilitating the selection of target sites in thegenome that contain Ftz/Ftz-F1 composite binding sites. Ftz, on the other hand, influences Ftz-F1 activity by interacting with its AF-2 domain in a manner that mimics a nuclear receptor coactivator. (C) 2001 Elsevier ScienceIreland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 07:18:23