Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro.
We have investigated the cleavages at the flavivirus capsid-prM protein junction in vitro. When expressed in the absence of the flavivirus proteinase, capsid and prM, which are separated by an internal signal sequence, exist as a membrane-spanning precursor protein. Here we show the induction of posttranslational signal peptidase cleavage of prM by trypsin cleavage of a cytoplasmic region of this precursor protein.
D000818:Animals; D001345:Autoradiography; D002213:Capsid / Q000096:biosynthesis*; D002460:Cell Line; D003545:Cysteine / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D005416:Flavivirus / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism; D007700:Kinetics; D008565:Membrane Proteins; D008715:Methionine / Q000378:metabolism; D008861:Microsomes / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases; D013462:Sulfur Radioisotopes; D014759:Viral Envelope Proteins / Q000096:biosynthesis*
D008565:Membrane Proteins; D011498:Protein Precursors; D013462:Sulfur Radioisotopes; D014759:Viral Envelope Proteins; C074932:prM protein, Flavivirus; D008715:Methionine; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase; D003545:Cysteine