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  • Title: Prohormone processing in Xenopus oocytes: characterization of cleavage signals and cleavage enzymes.
    Author: Korner J, Chun J, O'Bryan L, Axel R.
    Journal: Proc Natl Acad Sci U S A; 1991 Dec 15; 88(24):11393-7. PubMed ID: 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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