Albumins and their processing machinery are hijacked for cyclic peptides in sunflower

Nat Chem Biol. 2011 May;7(5):257-9. doi: 10.1038/nchembio.542. Epub 2011 Mar 20.

Abstract

The cyclic peptide sunflower trypsin inhibitor 1 (SFTI-1) blocks trypsin and is a promising drug lead and protein engineering scaffold. We show that SFTI-1 and the newfound SFT-L1 are buried within PawS1 and PawS2, precursors for seed storage protein albumins. Proalbumins are matured by asparaginyl endopeptidase, which we show is required to liberate both ends of SFTI-1 as well as to mature PawS1 albumin. Thus, these peptides emerge from within an albumin precursor by the action of albumin's own processing enzyme.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Albumins / chemistry
  • Albumins / metabolism*
  • Amino Acid Sequence
  • Cysteine Endopeptidases / metabolism
  • Helianthus / chemistry
  • Helianthus / metabolism*
  • Molecular Sequence Data
  • Peptides, Cyclic / chemistry
  • Peptides, Cyclic / metabolism*
  • Prealbumin / metabolism
  • Seed Storage Proteins / chemistry
  • Seed Storage Proteins / metabolism
  • Trypsin Inhibitors / chemistry
  • Trypsin Inhibitors / pharmacology

Substances

  • Albumins
  • Peptides, Cyclic
  • Prealbumin
  • SFTI-1 peptide, sunflower
  • Seed Storage Proteins
  • Trypsin Inhibitors
  • Cysteine Endopeptidases
  • asparaginylendopeptidase

Associated data

  • GENBANK/FJ469149
  • GENBANK/FJ469150
  • GENBANK/FJ749263
  • GENBANK/FJ749264
  • GENBANK/FJ749265
  • GENBANK/GQ342690