Molecular Aspects of Yeast Morphogenesis

Cabib, Enrico

doi:10.1146/annurev.mi.29.100175.001203

Cited by 85 publications

(37 citation statements)

References 94 publications

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“…Occasionally, a pair of cells was observed with an extrusion of cytoplasmic material at their interface, an effect noted previously (3). It is known that polyoxin D inhibits chitin synthetase of S. cerevisiae (15), and chitin is known to be involved as an important component of the primary septum of this yeast (4). Thus, we conclude that the chaining which we observe at high drug concentrations is the result of the inhibition of septum formation between the mother and daughter cells.…”

supporting

confidence: 53%

Polyoxin D inhibits growth of zoopathogenic fungi

Becker¹,

Covert²,

Shenbagamurthi³

et al. 1983

Antimicrob Agents Chemother

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We demonstrated that polyoxin D at millimolar concentrations caused marked morphological alterations of the human pathogens Candida albicans and Cryptococcus neoformans. C. albicans incubated in the presence of this drug grew in long chains that were severely swollen. Polyoxin D inhibited the growth of C. neoformans and killed cells of both the yeast and the hyphal phase of C. albicans. These observations give the first evidence that polyoxin antibiotics can kill zoopathogenic fungi.

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supporting

confidence: 53%

Polyoxin D inhibits growth of zoopathogenic fungi

Becker¹,

Covert²,

Shenbagamurthi³

et al. 1983

Antimicrob Agents Chemother

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“…Basing on this consideration, we decided to determine where nuclear DNA ended up during SUP35-C repression. To perform this, we took advantage of the fact that mothers, but not daughters, have chitin rings, called also bud scars, that can be visualized by fluorescent microscopy using calcofluor white [Cabib, 1975]. We stained cells of the s2-H8 strain after 9 h growth on glucose medium with DAPI and calcofluor white.…”

Section: Depletion Of Erf3c Alters Nuclear Division and Segregationmentioning

confidence: 99%

Yeast polypeptide chain release factors eRF1 and eRF3 are involved in cytoskeleton organization and cell cycle regulation

Valouev

Kushnirov

Ter‐Avanesyan

2002

Cell Motil. Cytoskeleton

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Termination of translation in eukaryotes is controlled by two interacting polypeptide chain release factors, eRF1 and eRF3. eRF1 recognizes nonsense codons UAA, UAG, and UGA, while eRF3 stimulates polypeptide release from the ribosome in a GTP- and eRF1-dependent manner. In the yeast Saccharomyces cerevisiae, eRF1 and eRF3 are encoded by the SUP45 and SUP35 genes, respectively. Here we show that in yeast shortage of any one of the release factors was accompanied by a reduction in the levels of the other release factor and resulted in a substantial increase of nonsense codon readthrough. Besides, repression of the genes encoding these factors caused different effects on cell morphology. Repression of the SUP35 gene caused accumulation of cells of increased size with large buds. This was accompanied by the disappearance of actin cytoskeletal structures, impairment of the mitotic spindle structure, and defects in nuclei division and segregation in mitosis. The evolutionary conserved C-terminal domain of eRF3 similar to the elongation factor EF-1alpha was responsible for these effects. Repression of the SUP45 gene caused accumulation of unbudded cells with 2C and higher DNA content, indicating that DNA replication is uncoupled from budding. The data obtained suggest that eRF1 and eRF3 play additional, nontranslational roles in the yeast cell.

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“…Cabib and co-workers have utilized this system to investigate the mechanism whereby the synthesis of chitin is localized to a particular region of the cell (primary septum) and at a specific time in the cell cycle (budding). Their excellent studies have been reviewed in detail elsewhere and will only be summarized briefl y in this article (10,12);…”

Section: Polarity Expressionmentioning

confidence: 99%