Protein phosphatase 2A (PP2A) is a heterotrimeric serine/threonine phosphatase consisting of A and B regulatory subunits and a C catalytic subunit. PP2A regulates cellular events that include the cell cycle, nutrient sensing, p53 stability and various mitogenic signals. Our studies explored a less understood role of PP2A, meiosis, exploiting the yeast Saccharomyces cerevisiae as a model system. We demonstrate that PP2ACdc55 containing the human B/55 family B subunit ortholog, Cdc55, is required for progression through meiosis I. cdc55 null cells arrest prior to spore formation, yet enter the meiotic program as indicated by expression of early meiotic genes. Cells lacking Cdc55 remain mononucleated, express early and middle meiotic genes prematurely, and harbor defects in intergenic recombination, and premeiotic DNA replication. The meiosis I defect of cdc55 cells can not be suppressed by bypassing recombination, eliminating pachytene checkpoint function, or removal of inhibitory cyclin-dependent kinase phosphorylation. Elimination of the Rad9-dependent DNA damage checkpoint partially suppresses the meiosis I defect of cdc55 cells. We conclude PP2ACdc55 is required for the proper temporal coupling of multiple meiotic events and/or monitors these events to ensure their fidelity.
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Title
The role of protein phosphatase 2A during meiosis I in Saccharomyces cerevisiae
Creators
Jocelyn Kibbe Nolt
Contributors
Joseph T. Nickels (Advisor) - Drexel University, Drexel University (1970-)
Awarding Institution
Drexel University
Degree Awarded
Doctor of Philosophy (Ph.D.)
Publisher
Drexel University; Philadelphia, Pennsylvania
Number of pages
xiii, 154 pages
Resource Type
Dissertation
Language
English
Academic Unit
College of Medicine; Drexel University
Other Identifier
991021889097904721
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