Biochemical, immunochemical, and ultrastructural studies of protein storage in poplar( Populus × canadensis ‘robusta’) wood Article DOI:
Cite this article as: Sauter, J.J. & van Cleve, B. Planta (1991) 183: 92. doi:10.1007/BF00197572 Abstract
The seasonal changes in protein content have been followed in the wood of
Populus × canadensis Moench ‘ robusta’, both biochemically and electronmicroscopically at the cellular level. In the storage-parenchyma cells of the twig wood, 4–6 μg · mg −1 DW protein were deposited in the fall, parallel to the yellowing of leaves, and mobilized completely again during the outgrowth of buds in the spring. Environmental impacts on the leaves, e.g. a fungal attack and mechanical injury by a hurricane, were found to affect protein deposition in the wood considerably. Accumulation of protein bodies in the fall and their disappearance from the cells in the spring proceeded parallel to the changes in protein content measured biochemically, proving that these organelles are the main sites of protein storage in the wood parenchyma cells. Using immunogold labelling and an anti-32-kDa poplar storage-protein antibody the protein bodies were shown to be the exclusive sites of storage of a 32-kDa polypeptide. Transient changes in protein content were also observed during fall and winter. Because these changes coincided with changes in protein-body structure and with changes in the population of vesicles and-or tubular membrane cisternae of the cells, an exchange of nitrogen compounds from the storage pool into the structural protein of membranes possibly takes place during these periods. The structural events observed during proteolysis in spring are very similar to those found in seeds. The possible roles of small cytoplasmic vesicles found within protein bodies during proteolysis and of multimembraneous vacuolar compartments during membrane retrieval are discussed. Key words Populus (protein storage) Protein body (immunocytochemistry, ultrastructure) Protein storage Wood (protein storage) Abbreviations DW
sodium dodecyl sulfate-polyacrylamide gel electrophoresis
Dedicated to Professor Dr. Dr. Hans Marquardt on the occasion of his 80th birthday
The valuable technical assistance of Miss Sabine Karg and Miss Astrid Diercks is gratefully acknowledged. This work was supported by the Deutsche Forschungsgemeinschaft.
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