Sambucus nigra agglutinin is located in protein bodies in the phloem parenchyma of the bark

Greenwood, John S.; Stinissen, Hetty M.; Peumans, Willy J.; Chrispeels, M. J.

doi:10.1007/bf00391426

Cited by 66 publications

(39 citation statements)

References 13 publications

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“…acids, and anthocyanins [7,62,121]. They may store proteins; vacuolar storage proteins are most prominent in seeds but may also occur in many different vegetative tissues [27,31,32,106]. Previous concepts of vacuole biogenesis and function hypothesized that protein storage vacuoles represented portions of the central vacuole that subdivided as deposits of storage protein accumulated [17,115].…”

Section: Complexity Of Vacuoles In Plant Cellsmentioning

confidence: 99%

Sorting of proteins to vacuoles in plant cells

Neuhaus

Rogers

1998

Protein Trafficking in Plant Cells

132

149

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An individual plant cell may contain at least two functionally and structurally distinct types of vacuoles: protein storage vacuoles and lytic vacuoles. Presumably a cell that stores proteins in vacuoles must maintain these separate compartments to prevent exposure of the storage proteins to an acidified environment with active hydrolytic enzymes where they would be degraded. Thus, the organization of the secretory pathway in plant cells, which includes the vacuoles, has a fascinating complexity not anticipated from the extensive genetic and biochemical studies of the secretory pathway in yeast. Plant cells must generate the membranes to form two separate types of tonoplast, maintain them as separate organelles, and direct soluble proteins from the secretory flow specifically to one or the other via separate vesicular pathways. Individual soluble and membrane proteins must be recognized and sorted into one or the other pathway by distinct, specific mechanisms. Here we review the emerging picture of how separate plant vacuoles are organized structurally and how proteins are recognized and sorted to each type.

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Section: Complexity Of Vacuoles In Plant Cellsmentioning

confidence: 99%

Sorting of proteins to vacuoles in plant cells

Neuhaus

Rogers

1998

Protein Trafficking in Plant Cells

132

149

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“…Urea was added to aliquots containing 100 Mig of protein to a concentration of 9 M; then, the sample was mixed with an equal volume of 9.5 M urea, 2% (v/v) Nonidet P-40, 2% (v/v) ampholytes (1.6% pH range 5-7, 0.4% pH range 3-10, BioRad), and 5% /3-mercaptoethanol. NEPHGE gels were made according to the procedure of O'Farrell et al (14), using a 3% final concentration of ampholytes (pH 5-7) and a 1% final concentration of ampholytes (pH [3][4][5][6][7][8][9][10]. A time series of NEPHGE gels containing identical samples was performed and an optimum running time for the protein sample of 2 h at a constant 400 V was determined.…”

Section: Sds-pagementioning

confidence: 99%

“…Vegetative storage proteins have been isolated from various plant organs including soybean pods and leaves (19), potato and yam tubers (7,16), and roots of perennial weeds (4) and from the wood, bark, and leaves of temperate trees (6,8,17,21,24,26). In general, they are not homologous to seed storage proteins of the same species (19).…”

mentioning

confidence: 99%

“…In general, they are not homologous to seed storage proteins of the same species (19). Vegetative storage proteins have been localized in protein-storage vacuoles within parenchymal cells of vegetative tissues (6,8,23), the organelles being similar in both ontogeny and structure to protein bodies found in mature dicotyledonous seed storage parenchymal cells (5).…”

mentioning

confidence: 99%

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The 32-Kilodalton Vegetative Storage Protein of Salix microstachya Turz

Wetzel

Greenwood²

1991

Plant Physiol.

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A 32-kilodalton vegetative storage protein, found in Salix microstachya Turz. bark during the overwintering period, was purified and characterized using several polyacrylamide gel electrophoretic procedures. Solubility characteristics and amino acid analyses were also performed. The protein is water soluble, is glycosylated, has no disulfide-bonded subunits, but is composed of a family of isoelectric isomers. The majority of these isomers are basic. Characteristic of storage proteins, the protein is rich in glutamine/glutamate and asparagine/aspartate (28%), the basic nature of the isomers indicating that most of these amino acid residues are in the amide form. The protein was purified using preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis and antibodies raised in chickens. Immunoblot analysis suggested an annual cyclic nature of the accumulation and mobilization of this vegetative storage protein. Immunologically, it is related to a similar molecular weight protein found in the bark of Populus deftoides Marsh. but not to any overwintering storage proteins of the other hardwoods tested. Indirect immunolocalization revealed that the protein was sequestered in proteinstorage vacuoles in parenchymatous cells of the inner bark tissues of Salix during the winter months.

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“…Recently, specific storage proteins have been identified in vegetative tissues of deciduous trees such as elderberry and poplar (Greenwood et al 1986;Sauter etal.1988;Wetz~letal.1989). These vegetative storage proteins can represent up to 30% of the tissue protein in the overwintering trees and it is believed that they con- seasonal changes in the 30 kD protein ofDouglas-fir and the 30 kD and 27 kD proteins of interior spruce, it is possible that these proteins are accumulated for overwintering and used as a source of nutrition during early spring growth.…”

Section: Discussionmentioning

confidence: 99%