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Nuclear proteomic changes linked to soybean rust resistance

Cooper, Bret, Campbell, Kimberly B., Feng, Jian, Garrett, Wesley M., Frederick, Reid
Molecular bioSystems 2011 v.7 no.3 pp. 773
Glycine max, Phakopsora pachyrhizi, cultivars, disease resistance, gene expression regulation, genes, leaves, liquid chromatography, mass spectrometry, nuclear proteins, phosphoproteins, plant pathogenic fungi, plant proteins, proteomics, soybean rust, soybeans, statistics, transcription factors
Soybean rust, caused by the fungus Phakopsora pachyrhizi, is an emerging threat to the US soybean crop. In an effort to identify proteins that contribute to disease resistance in soybean we compared a susceptible Williams 82 cultivar to a resistant Williams 82 inbred isoline harboring the Rpp1 resistance gene (R-gene). Approximately 4975 proteins from nuclear preparations of leaves were detected using a high-throughput liquid chromatography-mass spectrometry method. Many of these proteins have predicted nuclear localization signals, have homology to transcription factors and other nuclear regulatory proteins, and are phosphorylated. Statistics of summed spectral counts revealed sets of proteins with differential accumulation changes between susceptible and resistant plants. These protein accumulation changes were compared to previously reported gene expression changes and very little overlap was found. Thus, it appears that numerous proteins are post-translationally affected in the nucleus after infection. To our knowledge, this is the first indication of large-scale proteomic change in a plant nucleus after infection. Furthermore, the data reveal distinct proteins under control of Rpp1 and show that this disease resistance gene regulates nuclear protein accumulation. These regulated proteins likely influence broader defense responses, and these data may facilitate the development of plants with improved resistance.