Publication Information
Nakagami et al., 2010
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Abstract
Plant Physiol. 2010 Jul;153(3):1161-74. doi: 10.1104/pp.110.157347. Epub 2010
May 13.
Large-scale comparative phosphoproteomics identifies conserved phosphorylation
sites in plants.
Nakagami H(1), Sugiyama N, Mochida K, Daudi A, Yoshida Y, Toyoda T, Tomita M,
Ishihama Y, Shirasu K.
Author information:
(1)RIKEN Plant Science Center, Tsurumi-ku, Yokohama 230-0045, Japan.
Knowledge of phosphorylation events and their regulation is crucial to
understand the functional biology of plants. Here, we report a large-scale
phosphoproteome analysis in the model monocot rice (Oryza sativa japonica
'Nipponbare'), an economically important crop. Using unfractionated whole-cell
lysates of rice cells, we identified 6,919 phosphopeptides from 3,393 proteins.
To investigate the conservation of phosphoproteomes between plant species, we
developed a novel phosphorylation-site evaluation method and performed a
comparative analysis of rice and Arabidopsis (Arabidopsis thaliana). The ratio
of tyrosine phosphorylation in the phosphoresidues of rice was equivalent to
those in Arabidopsis and human. Furthermore, despite the phylogenetic distance
and the use of different cell types, more than 50% of the phosphoproteins
identified in rice and Arabidopsis, which possessed ortholog(s), had an
orthologous phosphoprotein in the other species. Moreover, nearly half of the
phosphorylated orthologous pairs were phosphorylated at equivalent sites.
Further comparative analyses against the Medicago phosphoproteome also showed
similar results. These data provide direct evidence for conserved regulatory
mechanisms based on phosphorylation in plants. We also assessed the
phosphorylation sites on nucleotide-binding leucine-rich repeat proteins and
identified novel conserved phosphorylation sites that may regulate this class of
proteins.
DOI: 10.1104/pp.110.157347
PMCID: PMC2899915
PMID: 20466843 [Indexed for MEDLINE]
