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Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana
The seeds of higher plants accumulate large quantities of storage protein. During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determ...
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Published in: | Proceedings of the National Academy of Sciences - PNAS 2003-12, Vol.100 (26), p.16095-16100 |
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creator | Shimada, T Fuji, K Tamura, K Kondo, M Nishimura, M Hara-Nishimura, I |
description | The seeds of higher plants accumulate large quantities of storage protein. During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determine the sorting machinery for storage proteins have not been successful. Here we show that a type I membrane protein, AtVSR1/AtELP, of Arabidopsis functions as a sorting receptor for storage proteins. The atvsr1 mutant missorts storage proteins by secreting them from cells, resulting in an enlarged and electron-dense extracellular space in the seeds. The atvsr1 seeds have distorted cells and smaller protein storage vacuoles than do WT seeds, and atvsr1 seeds abnormally accumulate the precursors of two major storage proteins, 12S globulin and 2S albumin, together with the mature forms of these proteins. AtVSR1 was found to bind to the C-terminal peptide of 12S globulin in a Ca2+-dependent manner. These findings demonstrate a receptor-mediated transport of seed storage proteins to protein storage vacuoles in higher plants. |
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During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determine the sorting machinery for storage proteins have not been successful. Here we show that a type I membrane protein, AtVSR1/AtELP, of Arabidopsis functions as a sorting receptor for storage proteins. The atvsr1 mutant missorts storage proteins by secreting them from cells, resulting in an enlarged and electron-dense extracellular space in the seeds. The atvsr1 seeds have distorted cells and smaller protein storage vacuoles than do WT seeds, and atvsr1 seeds abnormally accumulate the precursors of two major storage proteins, 12S globulin and 2S albumin, together with the mature forms of these proteins. AtVSR1 was found to bind to the C-terminal peptide of 12S globulin in a Ca2+-dependent manner. 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During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determine the sorting machinery for storage proteins have not been successful. Here we show that a type I membrane protein, AtVSR1/AtELP, of Arabidopsis functions as a sorting receptor for storage proteins. The atvsr1 mutant missorts storage proteins by secreting them from cells, resulting in an enlarged and electron-dense extracellular space in the seeds. The atvsr1 seeds have distorted cells and smaller protein storage vacuoles than do WT seeds, and atvsr1 seeds abnormally accumulate the precursors of two major storage proteins, 12S globulin and 2S albumin, together with the mature forms of these proteins. AtVSR1 was found to bind to the C-terminal peptide of 12S globulin in a Ca2+-dependent manner. 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Fuji, K ; Tamura, K ; Kondo, M ; Nishimura, M ; Hara-Nishimura, I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c519t-3bce4277f8280f1391bed36db3dff3395510493ac5dd90017d9a0527ff60537f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Albumins</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - growth & development</topic><topic>Arabidopsis - physiology</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - physiology</topic><topic>Arabidopsis thaliana</topic><topic>Base Sequence</topic><topic>binding proteins</topic><topic>Biological Sciences</topic><topic>Botany</topic><topic>DNA Primers</topic><topic>DNA, Bacterial - genetics</topic><topic>Extracellular space</topic><topic>Flowers & plants</topic><topic>Gene Deletion</topic><topic>Germination</topic><topic>Globulins</topic><topic>knockout mutants</topic><topic>membrane proteins</topic><topic>Mutagenesis</topic><topic>Plant cells</topic><topic>plant proteins</topic><topic>Protein precursors</topic><topic>protein transport</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Seeds</topic><topic>Seeds - genetics</topic><topic>Seeds - physiology</topic><topic>Storage proteins</topic><topic>Vacuoles</topic><topic>Vacuoles - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shimada, T</creatorcontrib><creatorcontrib>Fuji, K</creatorcontrib><creatorcontrib>Tamura, K</creatorcontrib><creatorcontrib>Kondo, M</creatorcontrib><creatorcontrib>Nishimura, M</creatorcontrib><creatorcontrib>Hara-Nishimura, I</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shimada, T</au><au>Fuji, K</au><au>Tamura, K</au><au>Kondo, M</au><au>Nishimura, M</au><au>Hara-Nishimura, I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2003-12-23</date><risdate>2003</risdate><volume>100</volume><issue>26</issue><spage>16095</spage><epage>16100</epage><pages>16095-16100</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The seeds of higher plants accumulate large quantities of storage protein. During seed maturation, storage protein precursors synthesized on rough endoplasmic reticulum are sorted to protein storage vacuoles, where they are converted into the mature forms and accumulated. Previous attempts to determine the sorting machinery for storage proteins have not been successful. Here we show that a type I membrane protein, AtVSR1/AtELP, of Arabidopsis functions as a sorting receptor for storage proteins. The atvsr1 mutant missorts storage proteins by secreting them from cells, resulting in an enlarged and electron-dense extracellular space in the seeds. The atvsr1 seeds have distorted cells and smaller protein storage vacuoles than do WT seeds, and atvsr1 seeds abnormally accumulate the precursors of two major storage proteins, 12S globulin and 2S albumin, together with the mature forms of these proteins. AtVSR1 was found to bind to the C-terminal peptide of 12S globulin in a Ca2+-dependent manner. These findings demonstrate a receptor-mediated transport of seed storage proteins to protein storage vacuoles in higher plants.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>14657332</pmid><doi>10.1073/pnas.2530568100</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Albumins Arabidopsis - genetics Arabidopsis - growth & development Arabidopsis - physiology Arabidopsis Proteins - genetics Arabidopsis Proteins - physiology Arabidopsis thaliana Base Sequence binding proteins Biological Sciences Botany DNA Primers DNA, Bacterial - genetics Extracellular space Flowers & plants Gene Deletion Germination Globulins knockout mutants membrane proteins Mutagenesis Plant cells plant proteins Protein precursors protein transport Proteins Receptors Seeds Seeds - genetics Seeds - physiology Storage proteins Vacuoles Vacuoles - physiology |
title | Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana |
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