Plant Molecular Biology

, Volume 42, Issue 2, pp 329–333

Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata

Authors

  • Elizabeth A. Miller
    • Department of Biochemistry and GeneticsLaTrobe University
  • Marcus C.S. Lee
    • Department of Biochemistry and GeneticsLaTrobe University
  • Angela H.O. Atkinson
    • Department of Biochemistry and GeneticsLaTrobe University
  • Marilyn A. Anderson
    • Department of Biochemistry and GeneticsLaTrobe University
Article

DOI: 10.1023/A:1006305429013

Cite this article as:
Miller, E.A., Lee, M.C., Atkinson, A.H. et al. Plant Mol Biol (2000) 42: 329. doi:10.1023/A:1006305429013

Abstract

Proteinase inhibitors (PIs) of the potato type II family have been identified in a number of solanaceous species. Most family members have two PI domains which are specific for either chymotrypsin or trypsin. More recently family members have been described with three or six repeated PI domains. Here we describe a novel four-domain family member produced in the stigmas and leaves of the ornamental tobacco, Nicotiana alata, which has high sequence identity with a six-domain member from the same species. Both proteins are produced as precursors that enter the secretory pathway and are subsequently processed into a series of 6 kDa PIs. The four- and six-domain precursor proteins were isolated from immature stigmas and characterised by mass spectrometry which revealed that both proteins had been trimmed at the N-terminus, at a position corresponding to the predicted signal peptide cleavage site. Furthermore, no post-translational modifications were apparent.

Nicotiana alataproteinase inhibitor IIstigma

Copyright information

© Kluwer Academic Publishers 2000