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Plant Cell Advance Online Publication
Published on May 12, 2009; 10.1105/tpc.108.060434

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Received May 5, 2008
Returned for revision March 12, 2009
Accepted April 29, 2009

Dynamic Behavior of Arabidopsis eIF4A-III, Putative Core Protein of Exon Junction Complex: Fast Relocation to Nucleolus and Splicing Speckles under Hypoxia

O.A. Koroleva 1*, G. Calder 2, A.F. Pendle 2, S.H. Kim 3, D. Lewandowska 4, C.G. Simpson 4, I.M. Jones 5, J.W.S. Brown 6, and P.J. Shaw 2

1 Department of Cell Biology, John Innes Centre, Colney, Norwich NR4 7UH, United Kingdom; School of Biological Sciences, University of Reading, Whiteknights, Reading, RG6 6AS, United Kingdom
2 Department of Cell Biology, John Innes Centre, Colney, Norwich NR4 7UH, United Kingdom
3 Genetics Programme, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, Scotland, United Kingdom; Division of Biosciences and Bioinformatics, College of Natural Science, Myongji University, Yongin, Kyeongki-do 449-728, Korea
4 Genetics Programme, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, Scotland, United Kingdom
5 School of Biological Sciences, University of Reading, Whiteknights, Reading, RG6 6AS, United Kingdom
6 Genetics Programme, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, Scotland, United Kingdom; Division of Plant Sciences, University of Dundee, Invergowrie, Dundee DD2 5DA, United Kingdom

* To whom correspondence should be addressed. E-mail: o.koroleva{at}reading.ac.uk.

Here, we identify the Arabidopsis thaliana ortholog of the mammalian DEAD box helicase, eIF4A-III, the putative anchor protein of exon junction complex (EJC) on mRNA. Arabidopsis eIF4A-III interacts with an ortholog of the core EJC component, ALY/Ref, and colocalizes with other EJC components, such as Mago, Y14, and RNPS1, suggesting a similar function in EJC assembly to animal eIF4A-III. A green fluorescent protein (GFP)-eIF4A-III fusion protein showed localization to several subnuclear domains: to the nucleoplasm during normal growth and to the nucleolus and splicing speckles in response to hypoxia. Treatment with the respiratory inhibitor sodium azide produced an identical response to the hypoxia stress. Treatment with the proteasome inhibitor MG132 led to accumulation of GFP-eIF4A-III mainly in the nucleolus, suggesting that transition of eIF4A-III between subnuclear domains and/or accumulation in nuclear speckles is controlled by proteolysis-labile factors. As revealed by fluorescence recovery after photobleaching analysis, the nucleoplasmic fraction was highly mobile, while the speckles were the least mobile fractions, and the nucleolar fraction had an intermediate mobility. Sequestration of eIF4A-III into nuclear pools with different mobility is likely to reflect the transcriptional and mRNA processing state of the cell.




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S. H. Kim, M. Spensley, S. K. Choi, C. P. G. Calixto, A. F. Pendle, O. Koroleva, P. J. Shaw, and J. W. S. Brown
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Nucleic Acids Res., January 16, 2010; (2010) gkp1241v1.
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