Ultrastructure of <i>Saccharomyces cerevisiae</i> cells accumulating Golgi organelles

Svoboda, Augustín; Necas, O

doi:10.1002/jobm.3620271008

Cited by 20 publications

(19 citation statements)

References 12 publications

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“…Indeed, with careful sample preparation, stacked cisternae consisting of two to four membranous compartments can be found in S. cerevisiae cells (Moor and Muhlethaler, 1963;Svoboda and Piedra, 1983;Makarow, 1988), and similar compartments have been observed near the projections of cells responding to the mating pheromone, a-factor (Baba et al, 1989). More definitive Golgi structures, reminiscent of those found in mammalian cells, are apparent in strains with mutations that disrupt traffic through the secretory pathway (Novick et al, 1980Svoboda and Necas, 1987). Cells with alterations in the SEC7 or SEC14 genes, defects that impair protein transport through the Golgi complex, accumulate cup-shaped organelles (termed Berkeley bodies) throughout the cytoplasm (Novick et al, 1980).…”

Section: Introductionmentioning

confidence: 92%

“…Strains with conditional mutations in the SEC7 gene are defective in protein secretion and accumulate parallel stacks of as many as 11 Golgi-like cisternae Svoboda and Necas, 1987). The Sec7p has a predicted molecular mass of 227 kDa (Achstetter et al, 1988) and associates with the cytosolic surface of the membranes of the Golgi complex (Franzusoff et al, 1991a.…”

Section: Identification Of Yeast Golgi Complexes Usingmentioning

confidence: 99%

“…Conventional electron microscopy preparations have revealed few structures corresponding closely to the elaborate Golgi complexes found in higher cells (Svoboda and Piedra, 1983;Svoboda and Necas, 1987), yet yeast clearly have Golgi functions, as summarized below. Animal cells typically contain one Golgi complex (Novikoff et al, 1971;Rambourg et al, 1981) that consists of several parallel and functionally distinct membranous sacs in which the oligosaccharides that decorate secretory proteins are successively extended and modified (reviewed in Kornfeld and Kornfeld 1985).…”

Section: Introductionmentioning

confidence: 99%

“…Cells with alterations in the SEC7 or SEC14 genes, defects that impair protein transport through the Golgi complex, accumulate cup-shaped organelles (termed Berkeley bodies) throughout the cytoplasm (Novick et al, 1980). When conditional sec7 mutant strains are incubated at the restrictive temperature and in medium with low levels of glucose, Golgi-like complexes consisting of 2-11 parallel cisternae become conspicuous Svoboda and Necas, 1987).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy.

Preuss

Mulholland

Franzusoff

et al. 1992

MBoC

263

221

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The membrane compartments responsible for Golgi functions in wild-type Saccharomyces cerevisiae were identified and characterized by immunoelectron microscopy. Using improved fixation methods, Golgi compartments were identified by labeling with antibodies specific for alpha 1-6 mannose linkages, the Sec7 protein, or the Ypt1 protein. The compartments labeled by each of these antibodies appear as disk-like structures that are apparently surrounded by small vesicles. Yeast Golgi typically are seen as single, isolated cisternae, generally not arranged into parallel stacks. The location of the Golgi structures was monitored by immunoelectron microscopy through the yeast cell cycle. Several Golgi compartments, apparently randomly distributed, were always observed in mother cells. During the initiation of new daughter cells, additional Golgi structures cluster just below the site of bud emergence. These Golgi enter daughter cells at an early stage, raising the possibility that much of the bud's growth might be due to secretory vesicles formed as well as consumed entirely within the daughter. During cytokinesis, the Golgi compartments are concentrated near the site of cell wall synthesis. Clustering of Golgi both at the site of bud formation and at the cell septum suggests that these organelles might be directed toward sites of rapid cell surface growth.

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Section: Introductionmentioning

confidence: 92%

Section: Identification Of Yeast Golgi Complexes Usingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy.

Preuss

Mulholland

Franzusoff

et al. 1992

MBoC

263

221

View full text Add to dashboard Cite

show abstract

“…Mutations at the sec7 locus exert a dramatic effect on the transport of secretory, plasma membrane, vacuolar and endocytic marker molecules (Esmon et al, 1981;Stevens et al, 1982;Riezman, 1985). Whereas morphologically identifiable stacks of Golgi cisternae are seldom observed in wild-type S.cerevisiae, sec7 cells accumulate stacked and exaggerated cisternae at the restrictive temperature Svoboda and Necas, 1987). Secretory glycoproteins that accumulate within these cisternae are exported when cells are returned to a permissive temperature (Esmon et al, 1981;Novick et al, 1980;Brada and Schekman, 1988).…”

Section: Introductionmentioning

confidence: 99%

Functional compartments of the yeast Golgi apparatus are defined by the sec7 mutation.

1989

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The role of the SEC7 gene product in yeast intercompartmental protein transport was examined. A spectrum of N‐linked oligosaccharide structures, ranging from core to nearly complete outer chain carbohydrate, was observed on glycoproteins accumulated in secretion‐defective sec7 mutant cells. Terminal alpha 1‐3‐linked outer chain mannose residues failed to be added to N‐linked glycoproteins in sec7 cells at the restrictive temperature. These results suggest that outer chain glycosyl modifications do not occur within a single compartment. Additional evidence consistent with subdivision of the yeast Golgi apparatus came from a cell‐free glycoprotein transport reaction in which wild‐type membranes sustained outer chain carbohydrate growth up to, but not including, addition of alpha 1‐3 mannose residues. Golgi apparatus compartments may specialize in addition of distinct outer chain determinants. The SEC7 gene product was suggested to regulate protein transport between and from functional compartments of the yeast Golgi apparatus.

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Transformations of membrane-bound organelles insec14 mutants of the yeastsSaccharomyces cerevisiae andYarrowia lipolytica

et al. 1996

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Background In early descriptions of ultrastructural alterations of secretory (sec) mutants of the yeast Saccharomyces cerevisiae, two mutants, sec7 and sec14, were shown to produce cell structures, the so‐called Berkeley bodies thought at first to correspond to Golgi structures. In sec7 mutants grown at restrictive temperature, secretion granules soon disappeared, whereas networks of Golgi tubules increased in size and transformed into stacks of seven to eight flattened elements. At these time intervals, structures resembling Berkeley bodies appeared to be extensions of the endoplasmic reticulum (Rambourg et al., 1993). It is the purpose of the present study to examine by electron microscopy S. cerevisiae sec14 mutants and to compare the modifications along their secretory pathway with those occurring in a homologous mutant of Yarrowia lipolytica. Methods S. cerevisiae sec 14 mutant cells coming from exponentially growing cultures were examined either at 24°C or after shifting at 37°C for 0, 2, 5, 10, 15, 20, 30, 45, 60, 90, and 120 min. Y. lipolytica mutant cells were first cultured in YNB in 5000 medium and then transferred for 0, 6, 8, 12, 20, and 24 hr, in a phosphate‐buffered YPD medium, which allows wild cells to differentiate from yeast to mycelian form. In both cases, cells were fixed in 2% glutaraldehyde, treated for 15 min in 1% sodium metaperiodate, post‐fixed in reduced osmium, and embedded in Epon. To visualize the three‐dimensional configuration of cell organelles, stereopairs were prepared from sections stained with lead citrate and tilted at ± 15° from the 0° position of the goniometric stage of the electron microscope. Results In S. cerevisiae mutant cells shifted for 2 min at the restrictive temperature, faintly stained networks of thin anastomosed tubules were located at close proximity and often continuous with faintly stained ER cisternae. More intensely stained tubular networks with nodular dilations having the size of secretion granules were dispersed throughout the cytoplasm. Later on, the faintly stained ER elements and related tubular networks decreased in number, whereas the intensely stained nodular tubular networks increased in frequency. The incidence of secretion granules also increased and were distributed at random throughout the cytoplasm. Wide‐meshed, intensely stained fenestrated spheres were often encountered and increased in number, in parallel to the increase in the number of nodular tubular networks. At late time intervals, the fenestrated spheres decreased in number as they seemingly transformed into spherical bodies identical to vacuoles. In contrast to what occurred in S. cerevisiae sec14 mutant, the main ultrastructural modification observed in Y. lipolytica transferred to the YPD medium was the formation of deep plasma membrane invaginations. Conclusions It appears that two functionally homologous PI/PC transfer proteins (Sec14psc and Sec14pyl) control distinct physiological processes in the two sec14 mutants examined. Such differences are perhaps related to t...

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Ultrastructure of Saccharomyces cerevisiae cells accumulating Golgi organelles

Cited by 20 publications

References 12 publications

Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy.

Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy.

Functional compartments of the yeast Golgi apparatus are defined by the sec7 mutation.

Transformations of membrane-bound organelles insec14 mutants of the yeastsSaccharomyces cerevisiae andYarrowia lipolytica

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