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Saccharomyces cerevisiae

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Articles 31 - 34 of 34

Full-Text Articles in Molecular Biology

Erv26p Directs Pro-Alkaline Phosphatase Into Endoplasmic Reticulum–Derived Coat Protein Complex Ii Transport Vesicles, Catherine A. Bue, Christine M. Bentivoglio, Charles Barlowe Sep 2006

Erv26p Directs Pro-Alkaline Phosphatase Into Endoplasmic Reticulum–Derived Coat Protein Complex Ii Transport Vesicles, Catherine A. Bue, Christine M. Bentivoglio, Charles Barlowe

Dartmouth Scholarship

Secretory proteins are exported from the endoplasmic reticulum (ER) in transport vesicles formed by the coat protein complex II (COPII). We detected Erv26p as an integral membrane protein that was efficiently packaged into COPII vesicles and cycled between the ER and Golgi compartments. The erv26Δ mutant displayed a selective secretory defect in which the pro-form of vacuolar alkaline phosphatase (pro-ALP) accumulated in the ER, whereas other secretory proteins were transported at wild-type rates. In vitro budding experiments demonstrated that Erv26p was directly required for packaging of pro-ALP into COPII vesicles. Moreover, Erv26p was detected in a specific complex with pro-ALP …

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The Cell Cycle–Regulated Genes Of Schizosaccharomyces Pombe, Anna Oliva, Adan Rosebrock, Francisco Ferrezuelo, Haiying Chen, Saumyadipta Pyne, Steve Skiena, Bruce Futcher, Janet Leatherwood Jun 2005

The Cell Cycle–Regulated Genes Of Schizosaccharomyces Pombe, Anna Oliva, Adan Rosebrock, Francisco Ferrezuelo, Haiying Chen, Saumyadipta Pyne, Steve Skiena, Bruce Futcher, Janet Leatherwood

Department of Molecular Genetics and Microbiology Faculty Publications

Many genes are regulated as an innate part of the eukaryotic cell cycle, and a complex transcriptional network helps enable the cyclic behavior of dividing cells. This transcriptional network has been studied in Saccharomyces cerevisiae (budding yeast) and elsewhere. To provide more perspective on these regulatory mechanisms, we have used microarrays to measure gene expression through the cell cycle of Schizosaccharomyces pombe (fission yeast). The 750 genes with the most significant oscillations were identified and analyzed. There were two broad waves of cell cycle transcription, one in early/mid G2 phase, and the other near the G2/M transition. The early/mid G2 …

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Erv14p Directs A Transmembrane Secretory Protein Into Copii-Coated Transport Vesicles, Jacqueline Powers, Charles Barlowe Feb 2002

Erv14p Directs A Transmembrane Secretory Protein Into Copii-Coated Transport Vesicles, Jacqueline Powers, Charles Barlowe

Dartmouth Scholarship

Erv14p is a conserved integral membrane protein that traffics in COPII-coated vesicles and localizes to the early secretory pathway in yeast. Deletion of ERV14 causes a defect in polarized growth because Axl2p, a transmembrane secretory protein, accumulates in the endoplasmic reticulum and is not delivered to its site of function on the cell surface. Herein, we show that Erv14p is required for selection of Axl2p into COPII vesicles and for efficient formation of these vesicles. Erv14p binds to subunits of the COPII coat and binding depends on conserved residues in a cytoplasmically exposed loop domain of Erv14p. When mutations are …

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Nuclear Export Of 60s Ribosomal Subunits Depends On Xpo1p And Requires A Nuclear Export Sequence-Containing Factor, Nmd3p, That Associates With The Large Subunit Protein Rpl10p, Olivier Gadal, Daniela Strau, Jacques Kessl, Bernard Trumpower Feb 2001

Nuclear Export Of 60s Ribosomal Subunits Depends On Xpo1p And Requires A Nuclear Export Sequence-Containing Factor, Nmd3p, That Associates With The Large Subunit Protein Rpl10p, Olivier Gadal, Daniela Strau, Jacques Kessl, Bernard Trumpower

Dartmouth Scholarship

Nuclear export of ribosomes requires a subset of nucleoporins and the Ran system, but specific transport factors have not been identified. Using a large subunit reporter (Rpl25p-eGFP), we have isolated several temperature-sensitive ribosomal export (rix) mutants. One of these corresponds to the ribosomal protein Rpl10p, which interacts directly with Nmd3p, a conserved and essential protein associated with 60S subunits. We find that thermosensitive nmd3 mutants are impaired in large subunit export. Strikingly, Nmd3p shuttles between the nucleus and cytoplasm and is exported by the nuclear export receptor Xpo1p. Moreover, we show that export of 60S subunits is Xpo1p dependent. We …

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