A critical review of translation initiation factor eIF2α kinases in plants – regulating protein synthesis during stress
Tracey M. Immanuel A B , David R. Greenwood A B and Robin M. MacDiarmid A B C
+ Author Affiliations
- Author Affiliations
A The New Zealand Institute for Plant & Food Research Limited, Private Bag 92169, Auckland, 1142, New Zealand.
B School of Biological Sciences, the University of Auckland, Private Bag 92019, Auckland Mail Centre, Auckland, 1142, New Zealand.
C Corresponding author. Email: robin.macdiarmid@plantandfood.co.nz
Functional Plant Biology 39(9) 717-735 https://doi.org/10.1071/FP12116
Submitted: 16 April 2012 Accepted: 10 July 2012 Published: 20 August 2012
Abstract
Eukaryotic cells must cope with environmental stress. One type of general stress response is the downregulation of protein synthesis in order to conserve cellular resources. Protein synthesis is mainly regulated at the level of mRNA translation initiation and when the α subunit of eukaryotic translation initiation factor 2 (eIF2) is phosphorylated, protein synthesis is downregulated. Although eIF2 has the same translation initiation function in all eukaryotes, it is not known whether plants downregulate protein synthesis via eIF2α phosphorylation. Similarly, although there is evidence that plants possess eIF2α kinases, it is not known whether they operate in a similar manner to the well characterised mammalian and yeast eIF2α kinases. Two types of eIF2α kinases have been reported in plants, yet the full understanding of the plant eIF2α phosphorylation mechanism is still lacking. Here we review the current knowledge of the eIF2α phosphorylation mechanism within plants and discuss plant eIF2α, plant eIF2α kinase GCN2 and the data supporting and contradicting the hypothesis that a functional orthologue for the eIF2α kinase PKR, is present and functional in plants.
Additional keywords: Arabidopsis, GCN2, phosphorylation, PKR, plant, translation initiation.
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