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Wheat α-gliadin and high-molecular-weight glutenin subunit accumulate in different storage compartments of transgenic soybean seed
Wheat seed storage proteins (prolamins) are important for the grain quality because they provide a characteristic texture to wheat flour products. In wheat endosperm cells, prolamins are transported from the Endoplasmic reticulum to Protein storage vacuoles through two distinct pathways—a convention...
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| Published in: | Transgenic research 2022-02, Vol.31 (1), p.43-58 |
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| cites | cdi_FETCH-LOGICAL-c375t-7ac92d7d25070038bcb83d9b2911c28cff70fa5dee590cb982926c8a6875380f3 |
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| creator | Matsuoka, Yuki Yamada, Tetsuya Maruyama, Nobuyuki |
| description | Wheat seed storage proteins (prolamins) are important for the grain quality because they provide a characteristic texture to wheat flour products. In wheat endosperm cells, prolamins are transported from the Endoplasmic reticulum to Protein storage vacuoles through two distinct pathways—a conventional pathway passing through the Golgi apparatus and an unconventional Golgi-bypassing pathway during which prolamins accumulate in the ER lumen, forming Protein bodies. Unfortunately, transport studies conducted previously achieved limited success because of the seed-specificity of the latter pathway and the multigene architecture of prolamins. To overcome this difficulty, we expressed either of the two families of wheat prolamins, namely α-gliadin or High-molecular-weight subunit of glutenin, in soybean seed, which naturally lacks prolamin-like proteins. SDS-PAGE analysis indicated the successful expression of recombinant wheat prolamins in transgenic soybean seeds. Their accumulation states were quite different—α-gliadin accumulated with partial fragmentation whereas the HMW-glutenin subunit formed disulfide-crosslinked polymers without fragmentation. Immunoelectron microscopy of seed sections revealed that α-gliadin was transported to PSVs whereas HMW-glutenin was deposited in novel ER-derived compartments distinct from PSVs. Observation of a developmental stage of seed cells showed the involvement of post-Golgi Prevacuolar compartments in the transport of α-gliadin. In a similar stage of cells, deposits of HMW-glutenin surrounded by membranes studded with ribosomes were observed confirming the accumulation of this prolamin as ER-derived PBs. Subcellular fractionation analysis supported the electron microscopy observations. Our results should help in better understanding of molecular events during the transport of prolamins in wheat. |
| doi_str_mv | 10.1007/s11248-021-00279-2 |
| format | article |
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In wheat endosperm cells, prolamins are transported from the Endoplasmic reticulum to Protein storage vacuoles through two distinct pathways—a conventional pathway passing through the Golgi apparatus and an unconventional Golgi-bypassing pathway during which prolamins accumulate in the ER lumen, forming Protein bodies. Unfortunately, transport studies conducted previously achieved limited success because of the seed-specificity of the latter pathway and the multigene architecture of prolamins. To overcome this difficulty, we expressed either of the two families of wheat prolamins, namely α-gliadin or High-molecular-weight subunit of glutenin, in soybean seed, which naturally lacks prolamin-like proteins. SDS-PAGE analysis indicated the successful expression of recombinant wheat prolamins in transgenic soybean seeds. Their accumulation states were quite different—α-gliadin accumulated with partial fragmentation whereas the HMW-glutenin subunit formed disulfide-crosslinked polymers without fragmentation. Immunoelectron microscopy of seed sections revealed that α-gliadin was transported to PSVs whereas HMW-glutenin was deposited in novel ER-derived compartments distinct from PSVs. Observation of a developmental stage of seed cells showed the involvement of post-Golgi Prevacuolar compartments in the transport of α-gliadin. In a similar stage of cells, deposits of HMW-glutenin surrounded by membranes studded with ribosomes were observed confirming the accumulation of this prolamin as ER-derived PBs. Subcellular fractionation analysis supported the electron microscopy observations. Our results should help in better understanding of molecular events during the transport of prolamins in wheat.</description><identifier>ISSN: 0962-8819</identifier><identifier>EISSN: 1573-9368</identifier><identifier>DOI: 10.1007/s11248-021-00279-2</identifier><identifier>PMID: 34427836</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Animal Genetics and Genomics ; Biomedical and Life Sciences ; Biomedical Engineering/Biotechnology ; Electron microscopy ; Endoplasmic reticulum ; Endosperm ; Flour ; Gel electrophoresis ; Genetic Engineering ; Gliadin ; Gliadin - genetics ; Gliadin - metabolism ; Glutenin ; Glutens - genetics ; Glutens - metabolism ; Glycine max - genetics ; Glycine max - metabolism ; Golgi apparatus ; Immunoelectron microscopy ; Life Sciences ; Microscopy ; Molecular Medicine ; Original Paper ; Plant Genetics and Genomics ; Prolamins - genetics ; Prolamins - metabolism ; Protein transport ; Ribosomes ; Seeds ; Seeds - genetics ; Seeds - metabolism ; Sodium lauryl sulfate ; Soybeans ; Storage proteins ; Transgenics ; Triticum - genetics ; Triticum - metabolism ; Vacuoles</subject><ispartof>Transgenic research, 2022-02, Vol.31 (1), p.43-58</ispartof><rights>The Author(s), under exclusive licence to Springer Nature Switzerland AG 2021</rights><rights>2021. The Author(s), under exclusive licence to Springer Nature Switzerland AG.</rights><rights>The Author(s), under exclusive licence to Springer Nature Switzerland AG 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-7ac92d7d25070038bcb83d9b2911c28cff70fa5dee590cb982926c8a6875380f3</citedby><cites>FETCH-LOGICAL-c375t-7ac92d7d25070038bcb83d9b2911c28cff70fa5dee590cb982926c8a6875380f3</cites><orcidid>0000-0001-6671-4995 ; 0000-0002-1369-9629</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34427836$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Matsuoka, Yuki</creatorcontrib><creatorcontrib>Yamada, Tetsuya</creatorcontrib><creatorcontrib>Maruyama, Nobuyuki</creatorcontrib><title>Wheat α-gliadin and high-molecular-weight glutenin subunit accumulate in different storage compartments of transgenic soybean seed</title><title>Transgenic research</title><addtitle>Transgenic Res</addtitle><addtitle>Transgenic Res</addtitle><description>Wheat seed storage proteins (prolamins) are important for the grain quality because they provide a characteristic texture to wheat flour products. In wheat endosperm cells, prolamins are transported from the Endoplasmic reticulum to Protein storage vacuoles through two distinct pathways—a conventional pathway passing through the Golgi apparatus and an unconventional Golgi-bypassing pathway during which prolamins accumulate in the ER lumen, forming Protein bodies. Unfortunately, transport studies conducted previously achieved limited success because of the seed-specificity of the latter pathway and the multigene architecture of prolamins. To overcome this difficulty, we expressed either of the two families of wheat prolamins, namely α-gliadin or High-molecular-weight subunit of glutenin, in soybean seed, which naturally lacks prolamin-like proteins. SDS-PAGE analysis indicated the successful expression of recombinant wheat prolamins in transgenic soybean seeds. Their accumulation states were quite different—α-gliadin accumulated with partial fragmentation whereas the HMW-glutenin subunit formed disulfide-crosslinked polymers without fragmentation. Immunoelectron microscopy of seed sections revealed that α-gliadin was transported to PSVs whereas HMW-glutenin was deposited in novel ER-derived compartments distinct from PSVs. Observation of a developmental stage of seed cells showed the involvement of post-Golgi Prevacuolar compartments in the transport of α-gliadin. In a similar stage of cells, deposits of HMW-glutenin surrounded by membranes studded with ribosomes were observed confirming the accumulation of this prolamin as ER-derived PBs. Subcellular fractionation analysis supported the electron microscopy observations. Our results should help in better understanding of molecular events during the transport of prolamins in wheat.</description><subject>Animal Genetics and Genomics</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedical Engineering/Biotechnology</subject><subject>Electron microscopy</subject><subject>Endoplasmic reticulum</subject><subject>Endosperm</subject><subject>Flour</subject><subject>Gel electrophoresis</subject><subject>Genetic Engineering</subject><subject>Gliadin</subject><subject>Gliadin - genetics</subject><subject>Gliadin - metabolism</subject><subject>Glutenin</subject><subject>Glutens - genetics</subject><subject>Glutens - metabolism</subject><subject>Glycine max - genetics</subject><subject>Glycine max - metabolism</subject><subject>Golgi apparatus</subject><subject>Immunoelectron microscopy</subject><subject>Life Sciences</subject><subject>Microscopy</subject><subject>Molecular Medicine</subject><subject>Original Paper</subject><subject>Plant Genetics and Genomics</subject><subject>Prolamins - genetics</subject><subject>Prolamins - metabolism</subject><subject>Protein transport</subject><subject>Ribosomes</subject><subject>Seeds</subject><subject>Seeds - genetics</subject><subject>Seeds - metabolism</subject><subject>Sodium lauryl sulfate</subject><subject>Soybeans</subject><subject>Storage proteins</subject><subject>Transgenics</subject><subject>Triticum - genetics</subject><subject>Triticum - metabolism</subject><subject>Vacuoles</subject><issn>0962-8819</issn><issn>1573-9368</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNp9kc1uFSEYhonR2NPqDbgwJG7cYPmZGWBpGn-aNHFT45Iw8DFnmhk4AhPTtVfkjXhNRU_VxEVXhI_nfT6SF6EXjL5hlMrzwhjvFKGcEUq51IQ_QjvWS0G0GNRjtKN64EQppk_QaSk3lLaYEk_Rieg6LpUYduj7lz3Yin_-INMyWz9HbKPH-3nakzUt4LbFZvIN2r3iadkqxIaUbdziXLF1blsbUQG3qZ9DgAyx4lJTthNgl9aDzXVts4JTwDXbWKamcLik2xFsUwH4Z-hJsEuB5_fnGfr8_t31xUdy9enD5cXbK-KE7CuR1mnupec9lZQKNbpRCa9HrhlzXLkQJA229wC9pm7Uims-OGUHJXuhaBBn6PXRe8jp6walmnUuDpbFRkhbMbwfOibk0OuGvvoPvUlbju13hg98YEzQTjaKHymXUykZgjnkebX51jBqflVkjhWZVpH5XZHhLfTyXr2NK_i_kT-dNEAcgdKe4gT53-4HtHd9oZ7F</recordid><startdate>20220201</startdate><enddate>20220201</enddate><creator>Matsuoka, Yuki</creator><creator>Yamada, Tetsuya</creator><creator>Maruyama, Nobuyuki</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6671-4995</orcidid><orcidid>https://orcid.org/0000-0002-1369-9629</orcidid></search><sort><creationdate>20220201</creationdate><title>Wheat α-gliadin and high-molecular-weight glutenin subunit accumulate in different storage compartments of transgenic soybean seed</title><author>Matsuoka, Yuki ; Yamada, Tetsuya ; Maruyama, Nobuyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-7ac92d7d25070038bcb83d9b2911c28cff70fa5dee590cb982926c8a6875380f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Animal Genetics and Genomics</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedical Engineering/Biotechnology</topic><topic>Electron microscopy</topic><topic>Endoplasmic reticulum</topic><topic>Endosperm</topic><topic>Flour</topic><topic>Gel electrophoresis</topic><topic>Genetic Engineering</topic><topic>Gliadin</topic><topic>Gliadin - genetics</topic><topic>Gliadin - metabolism</topic><topic>Glutenin</topic><topic>Glutens - genetics</topic><topic>Glutens - metabolism</topic><topic>Glycine max - genetics</topic><topic>Glycine max - metabolism</topic><topic>Golgi apparatus</topic><topic>Immunoelectron microscopy</topic><topic>Life Sciences</topic><topic>Microscopy</topic><topic>Molecular Medicine</topic><topic>Original Paper</topic><topic>Plant Genetics and Genomics</topic><topic>Prolamins - genetics</topic><topic>Prolamins - metabolism</topic><topic>Protein transport</topic><topic>Ribosomes</topic><topic>Seeds</topic><topic>Seeds - genetics</topic><topic>Seeds - metabolism</topic><topic>Sodium lauryl sulfate</topic><topic>Soybeans</topic><topic>Storage proteins</topic><topic>Transgenics</topic><topic>Triticum - genetics</topic><topic>Triticum - metabolism</topic><topic>Vacuoles</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matsuoka, Yuki</creatorcontrib><creatorcontrib>Yamada, Tetsuya</creatorcontrib><creatorcontrib>Maruyama, Nobuyuki</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Transgenic research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matsuoka, Yuki</au><au>Yamada, Tetsuya</au><au>Maruyama, Nobuyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Wheat α-gliadin and high-molecular-weight glutenin subunit accumulate in different storage compartments of transgenic soybean seed</atitle><jtitle>Transgenic research</jtitle><stitle>Transgenic Res</stitle><addtitle>Transgenic Res</addtitle><date>2022-02-01</date><risdate>2022</risdate><volume>31</volume><issue>1</issue><spage>43</spage><epage>58</epage><pages>43-58</pages><issn>0962-8819</issn><eissn>1573-9368</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Wheat seed storage proteins (prolamins) are important for the grain quality because they provide a characteristic texture to wheat flour products. In wheat endosperm cells, prolamins are transported from the Endoplasmic reticulum to Protein storage vacuoles through two distinct pathways—a conventional pathway passing through the Golgi apparatus and an unconventional Golgi-bypassing pathway during which prolamins accumulate in the ER lumen, forming Protein bodies. Unfortunately, transport studies conducted previously achieved limited success because of the seed-specificity of the latter pathway and the multigene architecture of prolamins. To overcome this difficulty, we expressed either of the two families of wheat prolamins, namely α-gliadin or High-molecular-weight subunit of glutenin, in soybean seed, which naturally lacks prolamin-like proteins. SDS-PAGE analysis indicated the successful expression of recombinant wheat prolamins in transgenic soybean seeds. Their accumulation states were quite different—α-gliadin accumulated with partial fragmentation whereas the HMW-glutenin subunit formed disulfide-crosslinked polymers without fragmentation. Immunoelectron microscopy of seed sections revealed that α-gliadin was transported to PSVs whereas HMW-glutenin was deposited in novel ER-derived compartments distinct from PSVs. Observation of a developmental stage of seed cells showed the involvement of post-Golgi Prevacuolar compartments in the transport of α-gliadin. In a similar stage of cells, deposits of HMW-glutenin surrounded by membranes studded with ribosomes were observed confirming the accumulation of this prolamin as ER-derived PBs. Subcellular fractionation analysis supported the electron microscopy observations. Our results should help in better understanding of molecular events during the transport of prolamins in wheat.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>34427836</pmid><doi>10.1007/s11248-021-00279-2</doi><tpages>16</tpages><orcidid>https://orcid.org/0000-0001-6671-4995</orcidid><orcidid>https://orcid.org/0000-0002-1369-9629</orcidid></addata></record> |
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| subjects | Animal Genetics and Genomics Biomedical and Life Sciences Biomedical Engineering/Biotechnology Electron microscopy Endoplasmic reticulum Endosperm Flour Gel electrophoresis Genetic Engineering Gliadin Gliadin - genetics Gliadin - metabolism Glutenin Glutens - genetics Glutens - metabolism Glycine max - genetics Glycine max - metabolism Golgi apparatus Immunoelectron microscopy Life Sciences Microscopy Molecular Medicine Original Paper Plant Genetics and Genomics Prolamins - genetics Prolamins - metabolism Protein transport Ribosomes Seeds Seeds - genetics Seeds - metabolism Sodium lauryl sulfate Soybeans Storage proteins Transgenics Triticum - genetics Triticum - metabolism Vacuoles |
| title | Wheat α-gliadin and high-molecular-weight glutenin subunit accumulate in different storage compartments of transgenic soybean seed |
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