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GrainGenes Reference Report: PMB-41-363

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Reference	PMB-41-363
Title	Specific in vitro phosphorylation of plant eIF2alpha by eukaryotic eIF2alpha kinases
Journal	Plant Molecular Biology
Year	1999
Volume	41
Pages	363-370
Author	Chang LY Yang WY Browning K Roth D
Abstract	Summary: Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) is known to be an important translational control mechanism in all eukaryotes with the major exception of plants. Regulation of mammalian and yeast eIF2alpha activity is directly governed by specific phosphorylation on Ser-51. We now demonstrate that recombinant wheat wild-type (51S) but not mutant 51-Ala (51A) protein is phosphorylated by human PKR and yeast GCN2, which are defined eIF2alpha kinases. Further, only wheat wild-type eIF2alpha is a substrate for plant-encoded, double-stranded RNA-dependent kinase (pPKR) activity. Plant PKR and GCN2 phosphorylate recombinant yeast eIF2alpha 51S but not the 51A mutant demonstrating that pPKR has recognition site capability similar to established eIF2alpha kinases. A truncated version of wild-type wheat eIF2alpha containing 51S but not the KGYID motif is not phosphorylated by either hPKR or pPKR suggesting that this putative eIF2alpha kinase docking domain is essential for phosphorylation. Taken together, these results demonstrate the homology among eukaryotic eIF2alpha species and eIF2a kinases and support the presence of a plant eIF2alpha phosphorylation pathway
Keyword	[ Hide all but 1 of 23 ] alpha binding proteins domain enzyme activity homologies homology human in vitro initiation factor kinase mechanism mutant phosphorylation protein kinase recognition regulation ribosomes saccharomyces cerevisiae translation translational control triticum aestivum wild-type yeast

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