Fission yeast Schizosaccharomyces pombe as a producer and secretor of heterologous proteins
نویسندگان
چکیده
Microorganisms are widely used as producers of heterologous (foreign) proteins of medical or industrial interest. Bacteria are the most efficient producers, but they are not able to perform the posttranslational processing of eucaryotic proteins (folding, glycosylation, phosphorylation or removal of part of their initial sequence). Eucaryotic yeasts are able to do the post-translational processing and secrete heterologous eucaryotic proteins in their native, biologically functional form. Among yeasts, the fission yeast Schizosaccharomyces pombe has the advantage of being more similar to higher eucaryotes in many respects, but its heterologus protein production is still small compared to that of other yeasts such as Saccharomyces cerevisiae, Pichia pastoris or Kluyveromyces lactis. However, the good quality of proteins obtained so far makes fission yeast an interesting producer and efforts are being made by many researchers to modify the gemome of S. pombe in order to obtain better producers of proteins. This review presents these efforts up to date and describes expression systems, signaling peptides, posttranslational processing and secretion systems known in fission yeast, and the possible ways to increase their efficiency. The last paragraphs are dedicated to approaching methods and protocols of genomic modifications.
منابع مشابه
Comparative proteomic and transcriptomic profiling of the fission yeast Schizosaccharomyces pombe
The fission yeast Schizosaccharomyces pombe is a widely used model organism to study basic mechanisms of eukaryotic biology, but unlike other model organisms, its proteome remains largely uncharacterized. Using a shotgun proteomics approach based on multidimensional prefractionation and tandem mass spectrometry, we have detected approximately 30% of the theoretical fission yeast proteome. Apply...
متن کاملA galactosyltransferase from the fission yeast Schizosaccharomyces pombe
A membrane-associated galactosyltransferase has been purified to homogeneity from the fission yeast, Schizosaccharomyces pombe. The enzyme has a molecular weight of 61,000 and is capable of transfering galactose from UDP-galactose (UDP-Gal) to a variety of mannose-based acceptors to form an alpha-1,2 galactosyl mannoside linkage. Immunofluorescence localization of the protein is consistent with...
متن کاملConstruction of an expression vector for the fission yeast Schizosaccharomyces pombe.
We have isolated and characterized a S. pombe promoter using a functional heterologous gene product assay. Random S. pombe genomic fragments were cloned upstream from the promoterless 'lacZ gene and tested in vivo for their efficiency to promote expression of the beta-galactosidase protein in the fission yeast. An efficient S. pombe promoter called 54/1 was isolated and shown to drive up to 5% ...
متن کاملPurification of actin from fission yeast Schizosaccharomyces pombe and characterization of functional differences from muscle actin.
Fission yeast Schizosaccharomyces pombe is an important genetic model organism for studying the mechanisms of endocytosis and cytokinesis. However, most work on the biochemical properties of fission yeast actin-binding proteins has been done with skeletal muscle actin for matters of convenience. When simulations of mathematical models of the mechanism of endocytosis were compared with events in...
متن کاملUncleavable Nup98–Nup96 is functional in the fission yeast Schizosaccharomyces pombe
Essential nucleoporins Nup98 and Nup96 are coded by a single open reading frame, and produced by autopeptidase cleavage. The autocleavage site of Nup98-Nup96 is highly conserved in a wide range of organisms. To understand the importance of autocleavage, we examined a mutant that produces the Nup98-Nup96 joint molecule as a sole protein product of the nup189 (+) gene in the fission yeast Schizos...
متن کامل