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Titolo:
A two-hybrid system for transactivator bait proteins
Autore:
Hirst, M; Ho, C; Sabourin, L; Rudnicki, M; Penn, L; Sadowski, I;
Indirizzi:
Univ British Columbia, Dept Biochem & Mol Biol, Vancouver, BC V6T 1Z3, Canada Univ British Columbia Vancouver BC Canada V6T 1Z3 ver, BC V6T 1Z3, Canada Univ Toronto, Dept Med Biophys, Toronto, ON M5G 2M9, Canada Univ Toronto Toronto ON Canada M5G 2M9 ophys, Toronto, ON M5G 2M9, Canada Univ Toronto, Ontario Canc Inst, Toronto, ON M5G 2M9, Canada Univ TorontoToronto ON Canada M5G 2M9 Inst, Toronto, ON M5G 2M9, Canada Ottawa Gen Hosp, Res Inst, Ottawa, ON K1H 8L6, Canada Ottawa Gen Hosp Ottawa ON Canada K1H 8L6 Inst, Ottawa, ON K1H 8L6, Canada
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 15, volume: 98, anno: 2001,
pagine: 8726 - 8731
SICI:
0027-8424(20010717)98:15<8726:ATSFTB>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-POLYMERASE-II; TRANSCRIPTION FACTOR-TFIIB; ACIDIC ACTIVATION DOMAINS; TATA-BINDING PROTEIN; CHROMATIN STRUCTURE; SHUTTLE VECTORS; HISTONES H3; MYOD FAMILY; YEAST; GAL4;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Sadowski, I Univ British Columbia, Dept Biochem & Mol Biol, 2146 Hlth Sci Mall, Vancouver, BC V6T 1Z3, Canada Univ British Columbia 2146 Hlth Sci Mall Vancouver BC Canada V6T 1Z3
Citazione:
M. Hirst et al., "A two-hybrid system for transactivator bait proteins", P NAS US, 98(15), 2001, pp. 8726-8731

Abstract

We describe a two-hybrid strategy for detection of interactions with transactivator proteins. This repressed transactivator (RTA) system employs the N-terminal repression domain of the yeast general repressor TUP1. TUP1-GAL80 fusion proteins, when coexpressed with GAL4, are shown to inhibit transcription of GAL4-dependent reporter genes, This effect requires the C-terminal 30 residues of GAL4, which are required for interaction with GAL80 in vitro. Furthermore, repression of GAL transcription by TUP1-GAL80 requires SRB10, demonstrating that the TUP1 repression domain, in the context of a two-hybrid interaction, functions by the same mechanism as endogenous TUP1. Using this strategy, we demonstrate interactions between the mammalian basic helix-loop-helix proteins MyoD and E12, and between c-Myc and Bin-1. We havealso identified interacting clones from a TUP1-cDNA fusion expression library by using GAL4-VP16 as a bait fusion. These results demonstrate that RTAis generally applicable for identifying and characterizing interactions with transactivator proteins in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 10:32:50