Reference "The amino acid sequence of a protein from wheat kernel closely related to proteins involved in the mechanisms of plant defence"

Reference ID

9218

Title

The amino acid sequence of a protein from wheat kernel closely related to proteins involved in the mechanisms of plant defence

Source

Journal of protein chemistry, 1993, vol. 12, pp. 379-386

Authors (5)

Caruso-C	Caporale-C
Poerio-E	Facchiano-A
Buonocore-V

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.