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Vol. 16, Issue 1, 260-269, January 2005
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* John Innes Centre, Norwich NR4 7UH, United Kingdom;
Scottish Crop Research Institute, Dundee DD2 5DA, Scotland;
University of Dundee, Dundee DD1 5HN, Scotland; and
University of Southern Denmark, DK-5230 Odense, Denmark
Submitted September 9, 2004;
Accepted October 13, 2004
Monitoring Editor: Joseph Gall
The eukaryotic nucleolus is involved in ribosome biogenesis and a wide range of other RNA metabolism and cellular functions. An important step in the functional analysis of the nucleolus is to determine the complement of proteins of this nuclear compartment. Here, we describe the first proteomic analysis of plant (Arabidopsis thaliana) nucleoli, in which we have identified 217 proteins. This allows a direct comparison of the proteomes of an important nuclear structure between two widely divergent species: human and Arabidopsis. The comparison identified many common proteins, plant-specific proteins, proteins of unknown function found in both proteomes, and proteins that were nucleolar in plants but nonnucleolar in human. Seventy-two proteins were expressed as GFP fusions and 87% showed nucleolar or nucleolar-associated localization. In a striking and unexpected finding, we have identified six components of the postsplicing exon-junction complex (EJC) involved in mRNA export and nonsense-mediated decay (NMD)/mRNA surveillance. This association was confirmed by GFP-fusion protein localization. These results raise the possibility that in plants, nucleoli may have additional functions in mRNA export or surveillance.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
|| Corresponding author. E-mail address: peter.shaw{at}bbsrc.ac.uk.
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