Nucleic Acids Research, Vol 26, Issue 17 3977-3985, Copyright © 1998 by Oxford University Press
B Pinson, I Sagot, F Borne, OS Gabrielsen and B Daignan-Fornier
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. We show that
mutating the conserved tryptophan residues in the DNA binding domain of
Bas1p severely impairs in vivo activation of target genes and 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 expression of 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 mutating a 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 of Bas1p and show that it is not
affected by extracellular adenine.
ARTICLES
Mutations in the yeast Myb-like protein Bas1p resulting in discrimination between promoters in vivo but notin vitro
Institut de Biochimie et Genetique Cellulaires, CNRS UPR9026, 1 rue Camille Saint-Saens, F-33077 Bordeaux Cedex, France.
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