pubmed-article:15643056 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15643056 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:15643056 | lifeskim:mentions | umls-concept:C0007610 | lld:lifeskim |
pubmed-article:15643056 | lifeskim:mentions | umls-concept:C0025186 | lld:lifeskim |
pubmed-article:15643056 | lifeskim:mentions | umls-concept:C0164198 | lld:lifeskim |
pubmed-article:15643056 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:15643056 | lifeskim:mentions | umls-concept:C0392752 | lld:lifeskim |
pubmed-article:15643056 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:15643056 | pubmed:dateCreated | 2005-1-11 | lld:pubmed |
pubmed-article:15643056 | pubmed:abstractText | Cyclophilin A is conserved from yeast to humans and mediates the ability of cyclosporine to perturb signal transduction cascades via inhibition of calcineurin. Cyclophilin A also catalyzes cis-trans peptidyl-prolyl isomerization during protein folding or conformational changes; however, cyclophilin A is not essential in yeast or human cells, and the true biological functions of this highly conserved enzyme have remained enigmatic. In Saccharomyces cerevisiae, cyclophilin A becomes essential in cells compromised for the nuclear prolyl-isomerase Ess1, and cyclophilin A physically interacts with two nuclear histone deacetylase complexes, Sin3-Rpd3 and Set3C, which both control meiosis. Here we show that cyclophilin A is localized to the nucleus in yeast cells and governs the meiotic gene program to promote efficient sporulation. The prolyl-isomerase activity of cyclophilin A is required for this meiotic function. We document that cyclophilin A physically associates with the Set3C histone deacetylase and analyze in detail the structure of this protein-protein complex. Genetic studies support a model in which cyclophilin A controls meiosis via Set3C and an additional target. Our findings reveal a novel nuclear role for cyclophilin A in governing the transcriptional program required for the vegetative to meiotic developmental switch in budding yeast. | lld:pubmed |
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