ArticleJournal of experimental botany2009
A 64 kDa sucrose binding protein is membrane-associated and tonoplast-localized in developing mung bean seeds.
Article in Journal of experimental botany, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- High-Pressure Freezing and Low-Temperature Processing of Seeds for Electron Microscopy and Electron Tomography.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Successful transport to the vacuole of heterologously expressed mung bean 8S globulin occurs in seed but not in vegetative tissues.Journal of experimental botany · 2013Article
- Multivesicular bodies in developing tobacco seed and mung bean are functionally equivalent.Plant signaling & behavior · 2012Article
- Storage globulins pass through the Golgi apparatus and multivesicular bodies in the absence of dense vesicle formation during early stages of cotyledon development in mung bean.Journal of experimental botany · 2012Article
- QUASIMODO 3 (QUA3) is a putative homogalacturonan methyltransferase regulating cell wall biosynthesis in Arabidopsis suspension-cultured cells.Journal of experimental botany · 2011Article
- The BURP domain protein AtUSPL1 of Arabidopsis thaliana is destined to the protein storage vacuoles and overexpression of the cognate gene distorts seed development.Plant molecular biology · 2009Article
- Wortmannin induces homotypic fusion of plant prevacuolar compartments.Journal of experimental botany · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sucrose binding proteins (SBPs) were predicted to be membrane-associated, but have been shown to localize in the lumen of protein storage vacuoles of various seeds. In this study, a new 64 kDa SBP has been identified from developing mung bean (Vigna radiata) seeds (here termed VrSBP1) via MS/MS analysis and N-terminal amino acid sequencing analysis and specific antibodies were generated using purified VrSBP1 proteins. Western blot analysis with the new VrSBP1 antibodies showed that, similar to most seed storage proteins, VrSBP1 proteins accumulated during seed development and were subsequently mobilized once the mung bean seeds germinated. Immunogold electron microscope (EM) studies on ultra-thin sections of high-pressure freezing/frozen substituted developing mung bean cotyledons demonstrated that VrSBP1 was localized specifically to the tonoplast of the protein storage vacuole and to the limiting membrane of a novel putative prevacuolar compartment. Biochemical and subcellular fractionation studies further demonstrated that VrSBP1 proteins were membrane-associated in developing mung beans, consistent with their tonoplast localization. This study thus shows convincing evidence of tonoplast-localization of a plant SBP for its future functional characterization and provides a model of studying non-integral membrane proteins associated with the tonoplasts in plant cells.
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