Reference "Structural and antifungal properties of a pathogenesis-related protein from wheat kernel"

Reference ID

9220

Title

Structural and antifungal properties of a pathogenesis-related protein from wheat kernel

Source

Journal of protein chemistry, 1996, vol. 15, pp. 35-44

Authors (8)

Caruso-C	Caporale-C
Chilosi-G	Vacca-F
Bertini-L	Magro-P
Poerio-E	Buonocore-V

Abstract

We have purified and characterized a protein from the water-soluble fraction of
wheat kernel (Triticum aestivum cv. S. Pastore) consisting of a single
polypeptide chain blocked at its N-terminus by a pyroglutamate residue; the
complete amino acid sequence has been determined by automated sequence analysis
performed on peptide fragments obtained by enzymatic hydrolyses of the protein.
Homology studies have shown that this protein is very similar (97% sequence
identity) to the previously characterized wheatwin1 as well as to other members
of the pathogenesis-related (PR) proteins of class 4; in analogy with wheatwin1,
we have termed this protein wheatwin2. Both wheatwin1 and wheatwin2 have
specific antifugal activity toward the wide-host-range pathogen Botrytis cinerea
and the wheat-specific pathogenic fungi of wheat Fusarium culmorum and Fusarium
graminearum of groups 1 and 2. On the basis of their structural and functional
properties, wheatwin1 and wheatwin2 can be classified as members of the PR4
protein family; this represents the first report concerning the presence of this
kind of protein in wheat.