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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Lassa virus glycoprotein signal peptide displays a novel topology with an extended endoplasmic reticulum luminal region.

Lassa virus glycoprotein C (GP-C) is translated as a precursor (preGP-C) into the lumen of the endoplasmic reticulum (ER) and cotranslationally cleaved into the signal peptide and immature GP-C before GP-C is proteolytically processed into its subunits, GP-1 and GP-2, which form the mature virion spikes. The signal peptide of preGP-C comprises 58 amino acids and contains two distinct hydrophobic domains. Here, we show that each hydrophobic domain alone can insert preGP-C into the ER membrane. Furthermore, we demonstrate that the native signal peptide only uses the N-terminal hydrophobic domain for membrane insertion, exhibiting a novel type of a topology for signal peptides with an extended ER luminal part, which is essential for proteolytic processing of GP-C into GP-1 and GP-2.[1]

References

  1. Lassa virus glycoprotein signal peptide displays a novel topology with an extended endoplasmic reticulum luminal region. Eichler, R., Lenz, O., Strecker, T., Eickmann, M., Klenk, H.D., Garten, W. J. Biol. Chem. (2004) [Pubmed]
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