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. 1991 Dec 15;88(24):11393–11397. doi: 10.1073/pnas.88.24.11393

Prohormone processing in Xenopus oocytes: characterization of cleavage signals and cleavage enzymes.

J Korner 1, J Chun 1, L O'Bryan 1, R Axel 1
PMCID: PMC53141  PMID: 1722329

Abstract

In this study, we characterize the sequences required for the cleavage of prohormones in Xenopus oocytes. We demonstrate that the yeast alpha-factor and the Aplysia egg-laying hormone (ELH) precursors are not cleaved in oocytes following simple pairs of basic residues, such as Lys-Arg, but that the ELH precursor is cleaved following the consensus sequence Arg-Xaa-(Lys/Arg)-Arg. This motif is conserved among precursors that are cleaved in virtually all mammalian cell types. Mutations that generate this sequence in the alpha-factor prohormone also result in efficient processing within oocytes. Cleavage at this consensus sequence may be due to the action of the Xenopus homologues of mammalian furin.

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