Elongation factor eEF1B modulates functions of the release factors eRF1 and eRF3 and the efficiency of translation termination in yeast.

Background: Termination of translation in eukaryotes is controlled by two interacting polypeptide chain release factors, eRF1 and eRF3. While eRF1 recognizes nonsense codons, eRF3 facilitates polypeptide chain release from the ribosome in a GTP-dependent manner. Besides termination, both release factors have essential, but poorly characterized functions outside of translation.

[Caffeine sensitivity of the yeast Saccharomyces cerevisiae MCD4 mutant is related to alteration of calcium homeostasis and degradation of misfolded proteins].

The MCD4 gene of Saccharomyces cerevisiae encodes a protein involved in glycosylphosphatidylinositol (GPI) biosynthesis. However, some mutations in the MCD4 gene have pleiotropic effects that may not be related to the defects in GPI anchor synthesis. The ssu21 mutation in the MCD4 gene studied here causes sensitivity to caffeine.

Deletion of BGL2 results in an increased chitin level in the cell wall of Saccharomyces cerevisiae.

It is shown that the deletion of BGL2 gene leads to increase in chitin content in the cell wall of Saccharomyces cerevisiae. A part of the additional chitin can be removed from the bgl2Delta cell wall by alkali or trypsin treatment. Chitin synthase 1 (Chs1) activity was increased by 60 % in bgl2Delta mutant.

Sup35p yeast prion-like protein as an adapter for production of the Gag-p55 antigen of HIV-1 and the L-chain of botulinum neurotoxin in Saccharomyces cerevisiae.

Effective expression of the HIV-1 core protein Gag-p55 was obtained in Saccharomyces cerevisiae under control of the inducible UASgal/CYC1 promoter as a translational fusion with the prion-forming NM domain of the translation terminator Sup35p (eRF3) of S. cerevisiae. where only poor expression of the original-type Gag-p55 was observed.

Purification and characterization of P33 protein of Candida utilis homologous to bgl2p of Saccharomyces cerevisiae; comparative analysis of the role of these proteins in molecular organization of the yeast cell walls.

P33 protein was isolated from the cell walls of Candida utilis. Homology between P33 and Bgl2p proteins from the cell walls of Saccharomyces cerevisiae was shown. The important role of these proteins in molecular organization of yeast cell walls was demonstrated using trypsin proteolysis and the "gene disruption" method.