title: Prohevein is poorly processed but shows enhanced resistance to a chitin-binding fungus in transgenic tomato plants.
abstract: In latex of rubber tree (Hevea brasiliensis), prohevein, homologous to potato win gene-encoded proteins, is processed to yield mature hevein. This mature hevein is composed of one chitin-binding domain and the C-terminal polypeptide homologous to pathogenesis-related proteins such as tobacco PR-4 and tomato P2 proteins. In contrast, prohevein was poorly cleaved to form the C-terminal polypeptide in transgenic tomato plants expressing hevein gene (HEV1)-driven polypeptides. However, mature hevein, the N-terminal cleavage form, was not found in this system. Immunoblot analysis of extracellular and intracellular fluid proteins showed that HEV1-encoded polypeptides accumulated intracellularly. In addition, retardation of growth of Trichoderma hamatum was observed in transgenic tomatoes constitutively expressing HEV1-encoded proteins.
authors.affiliation: Department of Energy Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA.
authors.forename: H I
authors.initials: HI
authors.lastname: Lee
authors.forename: N V
authors.initials: NV
authors.lastname: Raikhel
mesh_terms: D000485:Allergens; D052179:Antigens, Plant; D023181:Antimicrobial Cationic Peptides; D002686:Chitin / Q000502:physiology*; D037102:Lectins / Q000235:genetics* / Q000378:metabolism; D018551:Solanum lycopersicum / Q000235:genetics*; D037121:Plant Lectins; D010940:Plant Proteins / Q000235:genetics* / Q000378:metabolism*; D030821:Plants, Genetically Modified / Q000235:genetics*; D011498:Protein Precursors / Q000378:metabolism*; D014242:Trichoderma / Q000502:physiology*
chemical_list: D000485:Allergens; D052179:Antigens, Plant; D023181:Antimicrobial Cationic Peptides; C097982:Hev b 6.01 protein, Hevea brasiliensis; D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; D011498:Protein Precursors; C045875:hevein; D002686:Chitin