Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro.
AUTOR(ES)
Stocks, C E
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=189766Documentos Relacionados
- Signal Peptidase Cleavage at the Flavivirus C-prM Junction: Dependence on the Viral NS2B-3 Protease for Efficient Processing Requires Determinants in C, the Signal Peptide, and prM
- Alterations of pr-M Cleavage and Virus Export in pr-M Junction Chimeric Dengue Viruses
- Activation of RuvC Holliday junction resolvase in vitro.
- Prolipoprotein signal peptidase of Escherichia coli requires a cysteine residue at the cleavage site.
- Post-translational cleavage of presecretory proteins with an extract of rough microsomes from dog pancreas containing signal peptidase activity.