Plant lipoxygenase 2 is a translation initiation factor-4E-binding protein

Citation
Ma. Freire et al., Plant lipoxygenase 2 is a translation initiation factor-4E-binding protein, PLANT MOL B, 44(2), 2000, pp. 129-140
Citations number
44
Categorie Soggetti
Plant Sciences","Animal & Plant Sciences
Journal title
PLANT MOLECULAR BIOLOGY
ISSN journal
01674412 → ACNP
Volume
44
Issue
2
Year of publication
2000
Pages
129 - 140
Database
ISI
SICI code
0167-4412(200009)44:2<129:PL2IAT>2.0.ZU;2-6
Abstract
The eukaryotic initiation factor 4E (eIF4E) emerged recently as a target fo r different types of regulation affecting translation. In animal and yeast cells, eIF4E-binding proteins modulate the availability of eIF4E. A search for plant eIF4E-binding proteins from Arabidopsis thaliana using the yeast genetic interaction system identified a clone encoding a lipoxygenase type 2 (AtLOX2). In vitro and in vivo biochemical assays confirm an interaction between AtLOX2 and plant eIF4E(iso) factor. A two-hybrid assay revealed tha t AtLOX2 is also able to interact with both wheat initiation factors 4E and 4E(iso). Deletion analysis maps the region of AtLOX2 involved in interacti on with AteIF(iso)4E between amino acids 175 and 232. A sequence related to the conserved motif present in several eIF4E-binding proteins was found in this region. Furthermore, the wheat p86 subunit, a component of the plant translation eIF(iso)4F complex, was found to interfere with the AteIF(iso)4 E-AtLOX2 interaction suggesting that p86 and AtLOX2 compete for the same si te on eIF(iso)4E. These results may reflect a link between eIF4Es factors m ediating translational control with LOX2 activity, which is probably conser ved throughout the plant kingdom.