Analysis of N-terminal processing of hepatitis C virus nonstructural protein 2.
We determined the partial amino (N)-terminal amino acid sequence of hepatitis C virus p21 (nonstructural protein 2 [NS2]). Cleavage at the p21 (NS2) N terminus depended on the presence of microsomal membranes. The amino-terminal position of p21 (NS2) was assigned to amino acid 810 of the hepatitis C virus strain IIJ precursor polyprotein. Mutation of the alanine residue at position P1 of the putative cleavage site inhibited membrane-dependent processing. This alteration in processing together with the fact that hydrophobic amino acid residues are clustered upstream of the putative cleavage site suggested the involvement of a signal peptidase(s) in the cleavage. Furthermore, mutation analysis of this possible cleavage site revealed the presence of another microsome membrane-dependent cleavage site upstream of the N terminus of p21 (NS2).
Mizushima
H
H
Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, Japan.
Hijikata
M
M
Tanji
Y
Y
Kimura
K
K
Shimotohno
K
K
D000595:Amino Acid Sequence; D001483:Base Sequence; D004252:DNA Mutational Analysis; D016174:Hepacivirus / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017421:Sequence Analysis; D013762:Tetrahydrofolate Dehydrogenase / Q000096:biosynthesis / Q000235:genetics; D017361:Viral Nonstructural Proteins / Q000235:genetics*
D011993:Recombinant Fusion Proteins; D017361:Viral Nonstructural Proteins; D013762:Tetrahydrofolate Dehydrogenase