Erschienen:
Springer Science and Business Media LLC, 2003
Erschienen in:EMBO reports
Sprache:
Englisch
DOI:
10.1038/sj.embor.7400002
ISSN:
1469-221X;
1469-3178
Entstehung:
Anmerkungen:
Beschreibung:
<jats:p>Lassa virus glycoprotein is translated as a precursor (pre‐GP‐C) into the lumen of the endoplasmic reticulum and is cotranslationally cleaved into the signal peptide and GP‐C, before GP‐C is proteolytically processed into its subunits GP1 and GP2. The signal peptide of pre‐GP‐C comprises 58 amino acids. The substitution of Lassa virus pre‐GP‐C signal peptide with another signal peptide still mediates translocation and the release of signal peptide but abolishes the proteolytic cleavage of GP‐C into GP1 and GP2. Remarkably, cleavage of GP‐C from these hybrid pre‐GP‐C substrates was restored on coexpression of the wild‐type pre‐GP‐C signal peptide, indicating that the signal peptide functions as a <jats:italic>trans</jats:italic>‐acting factor to promote Lassa virus GP‐C processing. To our knowledge, this is the first report on a signal peptide that is essential for proteolytic processing of a secretory pathway protein.</jats:p>