ArticleNucleic acids research1990
Phosphorylation influences the binding of the yeast RAP1 protein to the upstream activating sequence of the PGK gene.
Article in Nucleic acids research, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Direct transactivator-transcription factor IID (TFIID) contacts drive yeast ribosomal protein gene transcription.The Journal of biological chemistry · 2010Article
- A combined expression-interaction model for inferring the temporal activity of transcription factors.Journal of computational biology : a journal of computational molecular cell biology · 2009Article
- Repression of rRNA synthesis due to a secretory defect requires the C-terminal silencing domain of Rap1p in Saccharomyces cerevisiae.Nucleic acids research · 2001Article
- The C-terminal silencing domain of Rap1p is essential for the repression of ribosomal protein genes in response to a defect in the secretory pathway.Nucleic acids research · 1998Article
- Combinatorial regulation of the Saccharomyces cerevisiae CAR1 (arginase) promoter in response to multiple environmental signals.Molecular and cellular biology · 1996Article
- Article
- Phosphorylation of the Oxytricha telomere protein: possible cell cycle regulation.Nucleic acids research · 1995Article
- Nutrient availability and the RAS/cyclic AMP pathway both induce expression of ribosomal protein genes in Saccharomyces cerevisiae but by different mechanisms.Molecular and cellular biology · 1995Article
- Growth-related expression of ribosomal protein genes in Saccharomyces cerevisiae.Molecular & general genetics : MGG · 1993Article
- A transcriptionally active form of GAL4 is phosphorylated and associated with GAL80.Molecular and cellular biology · 1992Article
- Global regulators of chromosome function in yeast.Antonie van Leeuwenhoek · 1992Review
- Multifunctional DNA-binding proteins in yeast.Gene expression · 1992Review
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Yeast repressor activator protein 1 (RAP1) binds in vitro to specific DNA sequences that are found in diverse genetic elements. Expression of the yeast phosphoglycerate kinase gene (PGK) requires the binding of RAP1 to the activator core sequence within the upstream activating sequence (UAS) of PGK. A DNA fragment Z+ which contains the activator core sequence of the PGK(UAS) has been shown to bind RAP1. Here we report that phosphatase treatment of RAP1 affected its binding to the PGK(UAS) but that this depended on the nature of the sequence flanking the 5' end of the activator core sequence. When the sequence flanking the 5' end of the activator core sequence was different from the PGK RAP1-binding site, phosphatase treatment of RAP1 decreased its binding to the DNA. When the 5' end of the binding site was a match to the PGK RAP1-binding site dephosphorylation of RAP1 increased RAP1 binding to the DNA. These observations were reproduced when the minimal functional DNA-binding domain of the RAP1 protein was used, implicating a phosphorylation-dependent binding of RAP1. This is the first evidence for phosphorylation-dependent binding of RAP1.
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