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    Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11393-7.

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

    Korner J, Chun J, O'Bryan L, Axel R.

    Department of Biochemistry and Biophysics, Columbia University, New York, NY 10032.

    Erratum in:

    • Proc Natl Acad Sci U S A 1992 May 15;89(10):4779.

    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.

    PMID: 1722329 [PubMed - indexed for MEDLINE]

    PMCID: 53141

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