Autoprocessing of Drosophila copia gag precursor to generate a unique laminate structure in Escherichia coli.
Drosophila copia protease is likely to be encoded in the gag gene. We have expressed copia gag polyprotein precursor in E. coli. The gag precursor was correctly processed to generate a unique laminate structure in E. coli. The processing was almost completely blocked by a mutation at the putative active site of copia protease, and resulted in accumulation of the precursor. Furthermore, the laminate structure was not found in E. coli expressing the mutant precursor. These results indicate that the protease is involved in cleaving the gag precursor itself. Also, the assembly of copia gag protein should correlate to the autoprocessing of copia gag polyprotein precursor.
Yoshioka
K
K
Laboratory of Molecular Biology, School of Hygienic Sciences, Kitasato University, Kanagawa, Japan.
Kanda
H
H
Kondo
S
S
Togashi
S
S
Miyake
T
T
Shiba
T
T
D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D015153:Blotting, Western; D004251:DNA Transposable Elements; D004330:Drosophila / Q000235:genetics*; D010450:Endopeptidases / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D015683:Gene Products, gag / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000096:biosynthesis
D004251:DNA Transposable Elements; D015683:Gene Products, gag; D011498:Protein Precursors; D011994:Recombinant Proteins; D010450:Endopeptidases