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Titolo:
MUTATIONS IN THE YEAST MYB-LIKE PROTEIN BAS1P RESULTING IN DISCRIMINATION BETWEEN PROMOTERS IN-VIVO BUT NOT IN-VITRO
Autore:
PINSON B; SAGOT I; BORNE F; GABRIELSEN OS; DAIGNANFORNIER B;
Indirizzi:
CNRS,INST BIOCHIM & GENET CELLULAIRES,UPR9026,1 RUE CAMILLE ST SAENS F-33077 BORDEAUX FRANCE CNRS,INST BIOCHIM & GENET CELLULAIRES,UPR9026 F-33077 BORDEAUX FRANCE UNIV OSLO,DEPT BIOCHEM N-0316 OSLO NORWAY
Titolo Testata:
Nucleic acids research
fascicolo: 17, volume: 26, anno: 1998,
pagine: 3977 - 3985
SICI:
0305-1048(1998)26:17<3977:MITYMP>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTIONAL ACTIVATORS BAS1; C-MYB; HIS4 TRANSCRIPTION; BUDDING YEAST; DNA-BINDING; COMPLEX; GENES; MOTIF; IDENTIFICATION; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
B. Pinson et al., "MUTATIONS IN THE YEAST MYB-LIKE PROTEIN BAS1P RESULTING IN DISCRIMINATION BETWEEN PROMOTERS IN-VIVO BUT NOT IN-VITRO", Nucleic acids research, 26(17), 1998, pp. 3977-3985

Abstract

Bas1p is a yeast transcription factor that activates expression of purine and histidine biosynthesis genes in response to extracellular purine limitation. The N-terminal part of Bas1p contains an Myb-like DNA binding domain composed of three tryptophan-rich imperfect repeats. Weshow that mutating the conserved tryptophan residues in the DNA binding domain of Bas1p severely impairs in vivo activation of target genesand in vitro DNA binding of Bas1p. We also found that two mutations (H34L and W42A) in the first repeat make Bas1p discriminate between promoters in vivo. These two BAS1 mutants are able to activate expressionof an HIS4-lacZ fusion but not that of ADE1-lacZ or ADE17-lacZ fusions. Surprisingly, these mutant proteins bind equally well to the three promoters in vitro, suggesting that the mutations affect the interaction of Bas1p with some promoter-specific factor(s) in vivo. By mutatinga potential nucleotide binding site in the DNA binding domain of Bas1p, we also show that this motif does not play a major role in purine regulation of Bas1p activity. Finally, using a green fluorescence protein (GFP)-Bas1p fusion, we establish the strict nuclear localization ofBas1p and show that it is not affected by extracellular adenine.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 03:11:29