Abstract
The amino acid sequence of wheatwin1, a monomeric protein of 125 residues isolated from wheat kernel (variety S. Pastore), is reported. Wheatwin1 is highly homologous (95%) to barwin, a protein from barley seed, which was shown to be related to the C-terminal domain of two proteins encoded by the wound-induced genes win1 and win2 in potato and to a protein encoded by the same domain of the hevein gene (hev1) in rubber tree. Similarly to barwin, wheatwin1 contains six cysteine residues all linked in disulfide bridges and the N-terminal residue is pyroglutamate. Moreover, structural studies performed on wheatwin1 and win1 protein by predictive methods demonstrated that these proteins and barwin are closely related in the secondary structure also. The high level of homology found with the product of win1, win2, and hev1 genes strongly suggests that barwin and wheatwin1 play a common role in the mechanism of plant defence.
Original language | English |
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Pages (from-to) | 379-386 |
Number of pages | 8 |
Journal | Journal of Protein Chemistry |
Volume | 12 |
Issue number | 4 |
DOIs | |
Publication status | Published - Aug 1993 |
Keywords
- Amino acid sequence
- plant defence
- wheat
- wounding
ASJC Scopus subject areas
- Biochemistry