The identification of inducible cytoplasmic/nuclear carbohydrate-binding proteins urges to develop novel concepts about the role of plant lectins.
During the last few years compelling evidence has been presented for the occurrence of cytoplasmic/nuclear plant lectins that are not detectable in normal plants but are only induced upon application of well-defined stress conditions. Since both the regulation of the expression and the subcellular location indicate that these 'non-classical lectins' are good candidates to play a physiologically important role as mediators of specific protein-carbohydrate-interactions within the plant cell, a critical assessment is made of the impact of these findings on the development of novel concepts about the role of plant lectins. Based on an analysis of the biochemical, molecular and evolutionary data of a jasmonate-induced chitin-binding lectin from tobacco leaves and a salt/jasmonate-induced leaf lectin from rice it is concluded that these lectins most probably interact with endogenous glycans located within the cytoplasmic/nuclear compartment of the plant cell. Several working mechanisms are proposed to explain how these inducible lectins may fulfill an important regulatory or structural role in stressed cells. In addition, the question of the evolutionary relationship(s) between the newly discovered inducible lectins and their 'classical' constitutively expressed homologs is addressed. Evidence is presented that the 'non-classical lectins' represent the main evolutionary line and that some of their corresponding genes were used as templates for genes encoding storage protein-like 'classical' homologs.
Ghent University, Department of Molecular Biotechnology, Coupure links 653, 9000 Gent, Belgium. ElsJM.VanDamme@UGent.be
Els J M
EJ
Van Damme
Nausicaä
N
Lannoo
Elke
E
Fouquaert
Willy J
WJ
Peumans
D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism*; D037121:Plant Lectins / Q000737:chemistry / Q000145:classification / Q000502:physiology*; D010940:Plant Proteins / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D015398:Signal Transduction
D009687:Nuclear Proteins; D037121:Plant Lectins; D010940:Plant Proteins; D011956:Receptors, Cell Surface; C055213:saccharide-binding proteins