Expression of a VEGF-like protein from Parapoxvirus ovis in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.
We report on the expression of a VEGF-like protein encoded by Parapoxvirus ovis in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. We show that a lysine residue at amino acid position 2 (K2) is an important determinant for the stability of this protein in S. cerevisiae. Replacement of K2 by an arginine results in stabilization of the protein. This observation suggests that this lysine may be a target for ubiquitinylation, which is a prerequisite for proteasome-mediated protein degradation. Interestingly, in S. pombe the lysine (K2) has no influence on the stability of the protein. This result indicates that the two yeast species exhibit significant differences in their protein degradation pathways.
Kettner
K
K
Institute of Genetics, University of Technology Dresden, D-01062 Dresden, Germany.
Friederichs
S
S
Schlapp
T
T
Rödel
G
G
D000345:Affinity Labels; D006388:Hemagglutinins; D008239:Lysine; D010957:Plasmids; D011994:Recombinant Proteins / Q000378:metabolism; D012440:Saccharomyces / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D014764:Viral Proteins / Q000378:metabolism*
D000345:Affinity Labels; D006388:Hemagglutinins; D011994:Recombinant Proteins; C084758:VEGF-like protein, Orf virus; D014764:Viral Proteins; D008239:Lysine