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Proteomics of Nitrogen Remobilization in Poplar Bark

Nazrul Islam, Gen Li, Wesley M. Garrett, Rongshuang Lin, Ganesh Sriram, Bret Cooper, Gary D. Coleman
Journal of proteome research 2015 v.14 no.2 pp. 1112-1126
metabolism, proteome, serine, autumn, nitrogen, nitrogen cycle, shoots, spring, carboxypeptidases, trees, parenchyma (plant tissue), seasonal variation, wood anatomy, proteomics, aspartic proteinases, bark, storage proteins, enzyme activity, leaves, cysteine proteinases
Seasonal nitrogen (N) cycling in temperate deciduous trees involves the accumulation of bark storage proteins (BSPs) in phloem parenchyma and xylem ray cells. BSPs are anabolized using recycled N during autumn leaf senescence and later become a source of N during spring shoot growth as they are catabolized. Little is known about the catabolic processes involved in remobilization and reutilization of N from BSPs in trees. In this study, we used multidimensional protein identification technology (MudPIT) and spectral counting to identify protein changes that occur in the bark during BSP catabolism. A total of 4,178 proteins were identified from bark prior to and during BSP catabolism. The majority (62%) of the proteins were found during BSP catabolism, indicating extensive remodeling of the proteome during renewed shoot growth and N remobilization. Among these proteins were 30 proteases, the relative abundances of which increased during BSP catabolism. These proteases spanned a range of families including members of the papain-like cysteine proteases, serine carboxypeptidases, and aspartyl proteases. These data identify, for the first time, candidate proteases that could potentially provide hydrolase activity required for N remobilization from BSPs and provide the foundation for research to advance our knowledge of poplar N cycling.