Saccharomyces cerevisiae cell cycle.

Regulation of glucose metabolism in growing yeast cells

Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide.

Publisher Summary 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 chitin-binding proteins, the regulation of genes responsible for chitin metabolism, and, finally, the targeting of chitin metabolism for insect-control purposes. Chitin is the major polysaccharide present in insects and many other invertebrates as well as in several microbes, including fungi. It serves as the skeletal polysaccharide of several animal phyla, such as the Arthropoda, Annelida, Molluska, and Coelenterata. In several groups of fungi, chitin replaces cellulose as the structural polysaccharide. In insects, it is found in the body wall or cuticle, gut lining or peritrophic matrix (PM), salivary gland, trachea, eggshells, and muscle attachment points. In the course of evolution, insects have made excellent use of the rigidity and chemical stability of the polymeric chitin to assemble both hard and soft extracellular structures such as the cuticle (exoskeleton) and PM respectively, both of which enable insects to be protected from the environment while allowing for growth, mobility, respiration, and communication. All of these structures are primarily composites of chitin fibers and proteins with varying degrees of hydration and trace materials distributed along the structures.

Chitin Metabolism in Insects

https://mmbr.asm.org/content/mmbr/43/2/117.full.pdf

Biosynthesis of cell walls of fungi.

Ficoll-gradient fractionation of a metabolic lysate from yeast spheroplasts was used to prepare vacuole, mitochondria and cytosol fractions. Tryptophan synthase activity was exclusively found in the soluble fraction. Proteinases A, B and C as well as the tryptophan-synthase-inactivating activity were mainly found in the vacuole fraction. The heat-stable activities inhibiting proteinase and tryptophan-synthase-inactivating enzyme appeared in the soluble fraction. The subcellular separation of tryptophan synthase and the tryptophan-synthase-inactivating activities explains why in crude extracts from stationary yeast cells, high tryptophan synthase activities are observed in spite of high tryptophan-synthase-inactivating activity. The proteinases of a freshly prepared vacuole fraction from yeast spheroplasts are unable to inactivate externally added tryptophan synthase unless the organelles are disrupted by sonication or osmotic shock.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1974.tb03748.x

Andrej Hasilik

Papers

Compartmentation of the Tryptophan‐Synthase‐Proteolyzing System in Saccharomyces cerevisiae

Participation of the tryptophan synthase inactivating system from yeast in the activation of chitin synthase.

Studies on a tryptophan synthase inactivating system from yeast.