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Identification of regulatory proteins that might be involved in carbon catabolite repression of the aminopeptidase I gene of the yeast Saccharomyces cerevisiae
Author(s) -
Bordallo Javier,
Suárez-Rendueles Paz
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01259-2
Subject(s) - catabolite repression , saccharomyces cerevisiae , yeast , fed batch culture , biochemistry , aminopeptidase , identification (biology) , chemistry , psychological repression , gene , biology , gene expression , amino acid , fermentation , leucine , mutant , botany
Transcription of the vacuolar aminopeptidase yscI ( APE1 ) gene in Saccharomyces cerevisiae has previously been suggested to require the participation of a cis upstream activation sequence (UAS) involved in carbon catabolite repression that responds to glucose. To determine the structure of the APE1 UAS element, we used the 18‐bp sequence 5′‐ATGAAT‐TAGTCAGCTTCT‐3′ as the DNA‐binding site. Using gel mobility shift assays, we have identified a 78 kDa protein from yeast that binds specifically to both single and double‐stranded forms of the UAS DNA‐binding site. We have also identified a 48 kDa heterodimer from yeast that binds specifically to the single‐stranded form of the UAS and whose DNA binding activity is remarkably heat stable. Even though the APE1 UAS contains a consensus sequence for the binding of the yeast activator protein yAP1, the two DNA‐protein complexes could still be detected in a strain bearing a deletion in the YAP1 gene.