Activation of the kexin from Schizosaccharomyces pombe requires internal cleavage of its initially cleaved prosequence.

Molecular and Cellular Biology
D Powner, J Davey

Abstract

Members of the kexin family of processing enzymes are responsible for the cleavage of many proproteins during their transport through the secretory pathway. The enzymes themselves are made as inactive precursors, and we investigated the activation process by studying the maturation of Krp1, a kexin from the fission yeast Schizosaccharomyces pombe. Using a cell-free translation-translocation system prepared from Xenopus eggs, we found that Krp1 is made as a preproprotein that loses the presequence during translocation into the endoplasmic reticulum. The prosequence is also rapidly cleaved in a reaction that is autocatalytic and probably intramolecular and is inhibited by disruption of the P domain. Prosequence cleavage normally occurs at Arg-Tyr-Lys-Arg102/ (primary cleavage site) but can occur at Lys-Arg82 (internal cleavage site) and/or Trp-Arg99 when the basic residues are removed from the primary site. Cleavage of the prosequence is necessary but not sufficient for activation, and Krp1 is initially unable to process substrates presented in trans. Full activation is achieved after further incubation in the extract and is coincident with the addition of O-linked sugars. O glycosylation is not, however, essential for activity, ...Continue Reading

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Citations

Nov 27, 2004·Journal of Molecular Recognition : JMR·Rachel Daly, Milton T W Hearn
Dec 20, 2013·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Cuifang LiReiko Sugiura
Jun 2, 2000·Protein Expression and Purification·J B DenaultR Leduc
Jan 13, 1999·Yeast·J Davey
Feb 18, 2006·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Yi HeTakayoshi Kuno
Nov 30, 2012·The Journal of Biological Chemistry·Davide CavazziniSimone Ottonello

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