Publication Information
Jones et al., 2009
No external accession available
Abstract
J Proteomics. 2009 Apr 13;72(3):439-51. doi: 10.1016/j.jprot.2009.02.004. Epub
2009 Feb 24.
Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
thaliana.
Jones AM(1), MacLean D, Studholme DJ, Serna-Sanz A, Andreasson E, Rathjen JP,
Peck SC.
Author information:
(1)The Sainsbury Laboratory, Norwich Research Park, Colney Lane, Norwich, United
Kingdom. alex.jones@tsl.ac.uk
Phosphorylation is a ubiquitous regulatory mechanism, that governs the activity,
subcellular localisation and molecular interactions of proteins. To identify a
broad range of nuclear phosphoproteins from Arabidopsis thaliana, we enriched
for nuclei from suspension cell cultures and seedlings before extensive
fractionation and identification of phosphopeptides by mass spectrometry. We
identified 416 phosphopeptides from 345 proteins with high confidence. Our data
show that sub-cellular fractionation is an effective strategy for identifying
nuclear phosphoproteins, two thirds of our dataset are known or predicted to be
nuclear localised and one half of the nuclear localised proteins have novel
phosphorylation sites. We identified novel phosphorylation sites on
transcription factors, chromatin remodelling proteins, RNA silencing components
and the spliceosome. Intriguingly, we also identified phosphorylation sites on
several proteins associated with Golgi vesicle trafficking such as the exocyst
complex, and speculate that these may be involved in cell plate formation during
cytokinesis.
DOI: 10.1016/j.jprot.2009.02.004
PMID: 19245862 [Indexed for MEDLINE]
