Abstract
Female reproductive tissues of the ornamental tobacco amass high levels of serine proteinase inhibitors (PIs) for protection against pests and pathogens. These PIs are produced from a precursor protein composed of six repeats each with a protease reactive site. Here we show that proteolytic processing of the precursor generates five single-chain PIs and a remarkable two-chain inhibitor formed by disulfide-bond linkage of N- and C-terminal peptide fragments. Surprisingly, PI precursors adopt this circular structure regardless of the number of inhibitor domains, suggesting this bracelet-like conformation is characteristic of the widespread potato inhibitor II (Pot II) protein family.
| Original language | English |
|---|---|
| Pages (from-to) | 526-530 |
| Number of pages | 5 |
| Journal | Nature Structural Biology |
| Volume | 6 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 9 Jun 1999 |
| Externally published | Yes |