Assembly and intracellular transport of phaseolin, the major storage protein of Phaseolus vulgaris L
| Autor: | Roberto Bollini, Alessandro Vitale, Emanuela Pedrazzini, Giovanna Giovinazzo, Aldo Ceriotti, Anna Bielli |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
Glycosylation biology glycosylation Physiology Endoplasmic reticulum Phaseolus vulgaris L Plant Science Vacuole biology.organism_classification oligomerization chemistry.chemical_compound endoplasmic reticulum Phaseolin Biochemistry chemistry Storage protein Phaseolus Glycoprotein Agronomy and Crop Science Secretory pathway |
| Zdroj: | Journal of plant physiology 145 (1995): 648–653. doi:10.1016/S0176-1617(11)81277-0 info:cnr-pdr/source/autori:A. Ceriotti, E. Pedrazzini, A. Bielli, G. Giovinazzo, R. Bollini e A. Vitale/titolo:Assembly and intracellular transport of phaseolin, the major storage protein of Phaseolus vulgaris L./doi:10.1016%2FS0176-1617(11)81277-0/rivista:Journal of plant physiology (Print)/anno:1995/pagina_da:648/pagina_a:653/intervallo_pagine:648–653/volume:145 |
| DOI: | 10.1016/S0176-1617(11)81277-0 |
| Popis: | Summary Phaseolin is a trimeric glycoprotein that accumulates in the protein storage vacuoles of common bean (Phaseolus vulgaris L.) seeds. The resistance to proteolytic degradation is likely to be an important feature of native phaseolin, allowing its stable accumulation in the protein storage vacuoles. Acquisition of a protease-resistant structure is linked to the assembly of phaseolin subunits into trimers, a rapid and efficient process occurring in the endoplasmic reticulum. In bean cotyledonary cells phaseolin trimerization is likely to be assisted by cellular factors and occurs also in the presence of inhibitors of N-linked glycosylation. A mechanism devoted to the retention of unassembled subunits and of assembly intermediates in an early compartment of the secretory pathway would guarantee that only the protease-resistant form of the protein is transported to the storage vacuoles, contributing to the overall efficiency of storage protein accumulation. |
| Databáze: | OpenAIRE |
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