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Journal ArticleDOI

Inactivation of chitin synthase in Saccharomyces cerevisiae.

A Hasilik
- 01 Jan 1974 - 
- Vol. 101, Iss: 4, pp 295-301
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TLDR
A new model of the regulation is presented which accounts for the specific location as well as for termination of chitin synthesis during the budding cycle.
Abstract
The activity of chitin synthase extracted from whole cells of Saccharomyces cerevisiae shows reproducible changes during the course of batch cultivation. During exponential growth 5–10% of the enzyme occurs in the active form, whereas in the stationary phase no active enzyme can be detected. Of three yeast proteinases, A, B and C, only B is able to activate pre-chitin synthase and inactivate chitin synthase. A new model of the regulation is presented which accounts for the specific location as well as for termination of chitin synthesis during the budding cycle.

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Book ChapterDOI

Chitin Metabolism in Insects

TL;DR: This chapter highlights some of the recent and important findings obtained from studies conducted on the synthesis, structure, physical state, modification, organization, and degradation of chitin in insect tissues, as well as the interplay of Chitin with chit in-binding proteins, the regulation of genes responsible for chitIn metabolism, and, finally, the targeting of chItin metabolism for insect-control purposes.
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Biosynthesis of cell walls of fungi.

TL;DR: A large number of the Wall Components studied had polysaccharide-protein complexes, and the structure of these complexes was similar to that of a cell wall, suggesting that wall architecture and structure-based determinants of wall growth and stability are similar.
Journal ArticleDOI

Solubilization and partial purification of yeast chitin synthetase. Confirmation of the zymogenic nature of the enzyme.

TL;DR: Chitin synthetase was solubilized with digitonin from a particulate yeast fraction and catalyzed the formation of insoluble chitin in the absence of added primer, confirming that chit in the plasma membrane as a zymogen and that initiation of the chitIn septum occurs by localized activation of the enzyme.
Journal ArticleDOI

Proteolytic activation and inactivation of chitin synthetase from Mucor rouxii.

TL;DR: The different behaviour of chitin synthetases in crude extracts of mycelium and yeast cells is consistent with, and perhaps partially responsible for, the differences in wall construction between mycelial and yeast forms of M. rouxii.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI

The vacuole as the lysosome of the yeast cell

TL;DR: Vacuoles can be isolated by flotation from suspensions of lysed proto-plasts in the presence of Ficoll by demonstrating the complete absence of enzymes of the mitochondria and of the groundplasm and by morphological observations.
Journal ArticleDOI

Chitin and yeast budding. Localization of chitin in yeast bud scars.

TL;DR: Yeast cells extracted with alkali and acetic acid revealed very thin cell envelopes with prominent bud scars in the shape of a shallow crater with a raised rim, which concluded that chitin is localized in a ring around the bud scar, sandwiched between two layers of glucan.
Journal ArticleDOI

Physical and chemical properties of polysaccharides and glycoproteins of the yeast-cell wall

TL;DR: Wright, B. E. & Shockman, G. D. (1955).
Journal ArticleDOI

The Control of Morphogenesis: An Enzymatic Mechanism for the Initiation of Septum Formation in Yeast

TL;DR: It is proposed that chitin synthetase, in the zymogen form, is uniformly distributed on the cytoplasmic membrane and at the time of septum initiation, vesicles carrying the activating factor would be directed to specific sites and bring about the localized conversion of theZymogen into the active form.
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