| Title: | Prohormone processing in Xenopus oocytes: characterization of cleavage signals and cleavage enzymes |
| Author(s): | Korner J; Chun J; O'Bryan L; Axel R; |
| Address: | "Department of Biochemistry and Biophysics, Columbia University, New York, NY 10032" |
| ISSN/ISBN: | 0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking) |
| 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" |
| Keywords: | "Amino Acid Sequence Animals Aplysia Base Sequence Cloning, Molecular Endopeptidases/*metabolism Furin Humans Invertebrate Hormones/*genetics Mating Factor Microinjections Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Oocytes;" |
| Notes: | "MedlineKorner, J Chun, J O'Bryan, L Axel, R eng P01 CA23767/CA/NCI NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1991/12/15 Proc Natl Acad Sci U S A. 1991 Dec 15; 88(24):11393-7. doi: 10.1073/pnas.88.24.11393" |
