ArticleEukaryotic cell2005
Disruption of histone deacetylase gene RPD3 accelerates PHO5 activation kinetics through inappropriate Pho84p recycling.
Article in Eukaryotic cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- The nicotinamide mononucleotide adenylyl transferase (NMNAT/Nma1) modulates phosphate-sensing (PHO) signaling independent of its NAD+ synthesis activity in Saccharomyces cerevisiae.FEMS yeast research · 2026Article
- The Histone Deacetylases Hst1 and Rpd3 Integrate De Novo NADInternational journal of molecular sciences · 2023Article
- The Rpd3-Complex Regulates Expression of Multiple Cell Surface Recycling Factors in Yeast.International journal of molecular sciences · 2021Article
- The yeast PHO5 promoter: from single locus to systems biology of a paradigm for gene regulation through chromatin.Nucleic acids research · 2014Review
- Targeted INO80 enhances subnuclear chromatin movement and ectopic homologous recombination.Genes & development · 2012Article
- Inorganic phosphate as an important regulator of phosphatases.Enzyme research · 2011Article
- Coupling phosphate homeostasis to cell cycle-specific transcription: mitotic activation of Saccharomyces cerevisiae PHO5 by Mcm1 and Forkhead proteins.Molecular and cellular biology · 2009Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The histone deacetylase Rpd3p functions as a transcriptional repressor of a diverse set of genes, including PHO5. Here we describe a novel role for RPD3 in the regulation of phosphate transporter Pho84p retention in the cytoplasmic membrane. We show that under repressing conditions (with P(i)), PHO5 expression is increased in a pho4Delta rpd3Delta strain, demonstrating PHO regulatory pathway independence. However, the effect of RPD3 disruption on PHO5 activation kinetics is dependent on the PHO regulatory pathway. Upon switching to activating conditions (without P(i)), PHO5 transcripts accumulated more rapidly in rpd3Delta cells. This more rapid response correlates with a defect in phosphate uptake due to premature recycling of Pho84p, the high-affinity H+/PO4(3-) symporter. Thus, RPD3 also participates in PHO5 regulation through a previously unidentified effect on maintenance of high-affinity phosphate uptake during phosphate starvation. We propose that Rpd3p has a negative role in the regulation of Pho84p endocytosis.
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