Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae.
Journal Article (Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Arévalo-Rodríguez, M; Heitman, J
Published Date
- January 2005
Published In
Volume / Issue
- 4 / 1
Start / End Page
- 17 - 29
PubMed ID
- 15643056
Pubmed Central ID
- PMC544151
International Standard Serial Number (ISSN)
- 1535-9778
Digital Object Identifier (DOI)
- 10.1128/EC.4.1.17-29.2005
Language
- eng
Conference Location
- United States