Stable synthesis of viral protein 2 of infectious bursal disease virus in Saccharomyces cerevisiae.
Viral protein 2 (VP2) from infectious bursal disease virus and its precursor polyprotein (N-VP2-VP4-VP3-C), in the absence of their native N-terminal region (19 amino acids), required fusion of yeast presequences for their stable synthesis in Saccharomyces cerevisiae [Jagadish et al., Gene 95 (1990) 179-186]. Restoration of the missing 19 aa resulted in stable synthesis of VP2, indicating the significance of the N-terminal region in protein stability.
Jagadish
M N
MN
CSIRO, Division of Biomolecular Engineering, Parkville Laboratory, Victoria, Australia.
Laughton
D L
DL
Azad
A A
AA
Macreadie
I G
IG
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D001483:Base Sequence; D015153:Blotting, Western; D004252:DNA Mutational Analysis; D015870:Gene Expression; D007243:Infectious bursal disease virus / Q000235:genetics*; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics
D000911:Antibodies, Monoclonal; D011498:Protein Precursors; D011994:Recombinant Proteins; D014764:Viral Proteins