A galactosyltransferase acting on arabinogalactan protein glycans is essential for embryo development in Arabidopsis
Summary Arabinogalactan proteins (AGPs) are a complex family of cell‐wall proteoglycans that are thought to play major roles in plant growth and development. Genetic approaches to studying AGP function have met limited success so far, presumably due to redundancy within the large gene families encod...
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Veröffentlicht in: | The Plant journal : for cell and molecular biology 2013-10, Vol.76 (1), p.128-137 |
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creator | Geshi, Naomi Johansen, Jorunn N. Dilokpimol, Adiphol Rolland, Aurélia Belcram, Katia Verger, Stéphane Kotake, Toshihisa Tsumuraya, Yoichi Kaneko, Satoshi Tryfona, Theodora Dupree, Paul Scheller, Henrik V. Höfte, Herman Mouille, Gregory |
description | Summary
Arabinogalactan proteins (AGPs) are a complex family of cell‐wall proteoglycans that are thought to play major roles in plant growth and development. Genetic approaches to studying AGP function have met limited success so far, presumably due to redundancy within the large gene families encoding AGP backbones. Here we used an alternative approach for genetic dissection of the role of AGPs in development by modifying their glycan side chains. We have identified an Arabidopsis glycosyltransferase of CAZY family GT31 (AtGALT31A) that galactosylates AGP side chains. A mutation in the AtGALT31A gene caused the arrest of embryo development at the globular stage. The presence of the transcript in the suspensor of globular‐stage embryos is consistent with a role for AtGALT31A in progression of embryo development beyond the globular stage. The first observable defect in the mutant is perturbation of the formative asymmetric division of the hypophysis, indicating an essential role for AGP proteoglycans in either specification of the hypophysis or orientation of the asymmetric division plane. |
doi_str_mv | 10.1111/tpj.12281 |
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Arabinogalactan proteins (AGPs) are a complex family of cell‐wall proteoglycans that are thought to play major roles in plant growth and development. Genetic approaches to studying AGP function have met limited success so far, presumably due to redundancy within the large gene families encoding AGP backbones. Here we used an alternative approach for genetic dissection of the role of AGPs in development by modifying their glycan side chains. We have identified an Arabidopsis glycosyltransferase of CAZY family GT31 (AtGALT31A) that galactosylates AGP side chains. A mutation in the AtGALT31A gene caused the arrest of embryo development at the globular stage. The presence of the transcript in the suspensor of globular‐stage embryos is consistent with a role for AtGALT31A in progression of embryo development beyond the globular stage. The first observable defect in the mutant is perturbation of the formative asymmetric division of the hypophysis, indicating an essential role for AGP proteoglycans in either specification of the hypophysis or orientation of the asymmetric division plane.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1111/tpj.12281</identifier><identifier>PMID: 23837821</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Agricultural sciences ; Amino Acid Sequence ; Arabidopsis - embryology ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabinogalactan proteins ; Cell Wall - metabolism ; Embryo development ; Embryos ; Flowers & plants ; Galactans - metabolism ; Galactosyltransferase ; Galactosyltransferases - genetics ; Galactosyltransferases - metabolism ; Gene Expression Regulation, Plant ; Genes ; Glycoproteins ; Life Sciences ; Mucoproteins - genetics ; Mucoproteins - metabolism ; Mutation ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Proteins ; Recombinant Proteins ; Transgenes</subject><ispartof>The Plant journal : for cell and molecular biology, 2013-10, Vol.76 (1), p.128-137</ispartof><rights>2013 The Authors The Plant Journal © 2013 John Wiley & Sons Ltd</rights><rights>2013 The Authors The Plant Journal © 2013 John Wiley & Sons Ltd.</rights><rights>Copyright © 2013 John Wiley & Sons Ltd and the Society for Experimental Biology</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-5828-745X ; 0000-0002-5493-754X ; 0000-0002-5728-146X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Ftpj.12281$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Ftpj.12281$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,315,781,785,886,1418,1434,27929,27930,45579,45580,46414,46838</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23837821$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01004321$$DView record in HAL$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1153388$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Geshi, Naomi</creatorcontrib><creatorcontrib>Johansen, Jorunn N.</creatorcontrib><creatorcontrib>Dilokpimol, Adiphol</creatorcontrib><creatorcontrib>Rolland, Aurélia</creatorcontrib><creatorcontrib>Belcram, Katia</creatorcontrib><creatorcontrib>Verger, Stéphane</creatorcontrib><creatorcontrib>Kotake, Toshihisa</creatorcontrib><creatorcontrib>Tsumuraya, Yoichi</creatorcontrib><creatorcontrib>Kaneko, Satoshi</creatorcontrib><creatorcontrib>Tryfona, Theodora</creatorcontrib><creatorcontrib>Dupree, Paul</creatorcontrib><creatorcontrib>Scheller, Henrik V.</creatorcontrib><creatorcontrib>Höfte, Herman</creatorcontrib><creatorcontrib>Mouille, Gregory</creatorcontrib><creatorcontrib>Joint Bioenergy Institute (JBEI)</creatorcontrib><title>A galactosyltransferase acting on arabinogalactan protein glycans is essential for embryo development in Arabidopsis</title><title>The Plant journal : for cell and molecular biology</title><addtitle>Plant J</addtitle><description>Summary
Arabinogalactan proteins (AGPs) are a complex family of cell‐wall proteoglycans that are thought to play major roles in plant growth and development. Genetic approaches to studying AGP function have met limited success so far, presumably due to redundancy within the large gene families encoding AGP backbones. Here we used an alternative approach for genetic dissection of the role of AGPs in development by modifying their glycan side chains. We have identified an Arabidopsis glycosyltransferase of CAZY family GT31 (AtGALT31A) that galactosylates AGP side chains. A mutation in the AtGALT31A gene caused the arrest of embryo development at the globular stage. The presence of the transcript in the suspensor of globular‐stage embryos is consistent with a role for AtGALT31A in progression of embryo development beyond the globular stage. The first observable defect in the mutant is perturbation of the formative asymmetric division of the hypophysis, indicating an essential role for AGP proteoglycans in either specification of the hypophysis or orientation of the asymmetric division plane.</description><subject>Agricultural sciences</subject><subject>Amino Acid Sequence</subject><subject>Arabidopsis - embryology</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabinogalactan proteins</subject><subject>Cell Wall - metabolism</subject><subject>Embryo development</subject><subject>Embryos</subject><subject>Flowers & plants</subject><subject>Galactans - metabolism</subject><subject>Galactosyltransferase</subject><subject>Galactosyltransferases - genetics</subject><subject>Galactosyltransferases - metabolism</subject><subject>Gene Expression Regulation, Plant</subject><subject>Genes</subject><subject>Glycoproteins</subject><subject>Life Sciences</subject><subject>Mucoproteins - genetics</subject><subject>Mucoproteins - metabolism</subject><subject>Mutation</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Proteins</subject><subject>Recombinant Proteins</subject><subject>Transgenes</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpd0UGP1CAUAGBiNO44evAPGKIXPXSXB21pj5ONuppJ9DAHb-SVMjNMKIyFWdN_L92ue5ADj7z35RF4hLwFdg153aTz6Ro4b-AZWYGoq0KA-PWcrFhbs0KWwK_IqxhPjIEUdfmSXHHRCNlwWJG0oQd0qFOIk0sj-rg3I0ZDc8r6Aw2e4oid9WFh6Ol5DMlYTw9u0tlTG6mJ0fhk0dF9GKkZunEKtDf3xoXzkCs0883cpg_naONr8mKPLpo3j3FNdl8-727viu2Pr99uN9viWLIaih7rruk10y3DEtqKM9GWvO6xzzsXwETJ98I0dSX7tpWiRdnLCiV0pm00ijV5v7QNMVkVtU1GH3Xw3uikACohmiajTws6olPn0Q44TiqgVXebrZpzDBgrBYd7yPbjYvMX_L6YmNRgozbOoTfhEhWUoqlkXee4Jh_-o6dwGX1-7awkb6Hks3r3qC7dYPqn-__NJ4ObBfyxzkxPdWBqHrzKg1cPg1e7n98fDuIv90qfAQ</recordid><startdate>201310</startdate><enddate>201310</enddate><creator>Geshi, Naomi</creator><creator>Johansen, Jorunn N.</creator><creator>Dilokpimol, Adiphol</creator><creator>Rolland, Aurélia</creator><creator>Belcram, Katia</creator><creator>Verger, Stéphane</creator><creator>Kotake, Toshihisa</creator><creator>Tsumuraya, Yoichi</creator><creator>Kaneko, Satoshi</creator><creator>Tryfona, Theodora</creator><creator>Dupree, Paul</creator><creator>Scheller, Henrik V.</creator><creator>Höfte, Herman</creator><creator>Mouille, Gregory</creator><general>Blackwell Publishing Ltd</general><general>Wiley</general><general>Blackwell</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>OTOTI</scope><orcidid>https://orcid.org/0000-0002-5828-745X</orcidid><orcidid>https://orcid.org/0000-0002-5493-754X</orcidid><orcidid>https://orcid.org/0000-0002-5728-146X</orcidid></search><sort><creationdate>201310</creationdate><title>A galactosyltransferase acting on arabinogalactan protein glycans is essential for embryo development in Arabidopsis</title><author>Geshi, Naomi ; Johansen, Jorunn N. ; Dilokpimol, Adiphol ; Rolland, Aurélia ; Belcram, Katia ; Verger, Stéphane ; Kotake, Toshihisa ; Tsumuraya, Yoichi ; Kaneko, Satoshi ; Tryfona, Theodora ; Dupree, Paul ; Scheller, Henrik V. ; Höfte, Herman ; Mouille, Gregory</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h4061-da6b8dc0c90a41952039426dad4262310342f3e8657d99739a7d75a71be98ca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Agricultural sciences</topic><topic>Amino Acid Sequence</topic><topic>Arabidopsis - embryology</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabinogalactan proteins</topic><topic>Cell Wall - metabolism</topic><topic>Embryo development</topic><topic>Embryos</topic><topic>Flowers & plants</topic><topic>Galactans - metabolism</topic><topic>Galactosyltransferase</topic><topic>Galactosyltransferases - genetics</topic><topic>Galactosyltransferases - metabolism</topic><topic>Gene Expression Regulation, Plant</topic><topic>Genes</topic><topic>Glycoproteins</topic><topic>Life Sciences</topic><topic>Mucoproteins - genetics</topic><topic>Mucoproteins - metabolism</topic><topic>Mutation</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Proteins</topic><topic>Recombinant Proteins</topic><topic>Transgenes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Geshi, Naomi</creatorcontrib><creatorcontrib>Johansen, Jorunn N.</creatorcontrib><creatorcontrib>Dilokpimol, Adiphol</creatorcontrib><creatorcontrib>Rolland, Aurélia</creatorcontrib><creatorcontrib>Belcram, Katia</creatorcontrib><creatorcontrib>Verger, Stéphane</creatorcontrib><creatorcontrib>Kotake, Toshihisa</creatorcontrib><creatorcontrib>Tsumuraya, Yoichi</creatorcontrib><creatorcontrib>Kaneko, Satoshi</creatorcontrib><creatorcontrib>Tryfona, Theodora</creatorcontrib><creatorcontrib>Dupree, Paul</creatorcontrib><creatorcontrib>Scheller, Henrik V.</creatorcontrib><creatorcontrib>Höfte, Herman</creatorcontrib><creatorcontrib>Mouille, Gregory</creatorcontrib><creatorcontrib>Joint Bioenergy Institute (JBEI)</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>OSTI.GOV</collection><jtitle>The Plant journal : for cell and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Geshi, Naomi</au><au>Johansen, Jorunn N.</au><au>Dilokpimol, Adiphol</au><au>Rolland, Aurélia</au><au>Belcram, Katia</au><au>Verger, Stéphane</au><au>Kotake, Toshihisa</au><au>Tsumuraya, Yoichi</au><au>Kaneko, Satoshi</au><au>Tryfona, Theodora</au><au>Dupree, Paul</au><au>Scheller, Henrik V.</au><au>Höfte, Herman</au><au>Mouille, Gregory</au><aucorp>Joint Bioenergy Institute (JBEI)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A galactosyltransferase acting on arabinogalactan protein glycans is essential for embryo development in Arabidopsis</atitle><jtitle>The Plant journal : for cell and molecular biology</jtitle><addtitle>Plant J</addtitle><date>2013-10</date><risdate>2013</risdate><volume>76</volume><issue>1</issue><spage>128</spage><epage>137</epage><pages>128-137</pages><issn>0960-7412</issn><eissn>1365-313X</eissn><abstract>Summary
Arabinogalactan proteins (AGPs) are a complex family of cell‐wall proteoglycans that are thought to play major roles in plant growth and development. Genetic approaches to studying AGP function have met limited success so far, presumably due to redundancy within the large gene families encoding AGP backbones. Here we used an alternative approach for genetic dissection of the role of AGPs in development by modifying their glycan side chains. We have identified an Arabidopsis glycosyltransferase of CAZY family GT31 (AtGALT31A) that galactosylates AGP side chains. A mutation in the AtGALT31A gene caused the arrest of embryo development at the globular stage. The presence of the transcript in the suspensor of globular‐stage embryos is consistent with a role for AtGALT31A in progression of embryo development beyond the globular stage. The first observable defect in the mutant is perturbation of the formative asymmetric division of the hypophysis, indicating an essential role for AGP proteoglycans in either specification of the hypophysis or orientation of the asymmetric division plane.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>23837821</pmid><doi>10.1111/tpj.12281</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-5828-745X</orcidid><orcidid>https://orcid.org/0000-0002-5493-754X</orcidid><orcidid>https://orcid.org/0000-0002-5728-146X</orcidid></addata></record> |
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subjects | Agricultural sciences Amino Acid Sequence Arabidopsis - embryology Arabidopsis - enzymology Arabidopsis - genetics Arabinogalactan proteins Cell Wall - metabolism Embryo development Embryos Flowers & plants Galactans - metabolism Galactosyltransferase Galactosyltransferases - genetics Galactosyltransferases - metabolism Gene Expression Regulation, Plant Genes Glycoproteins Life Sciences Mucoproteins - genetics Mucoproteins - metabolism Mutation Plant Proteins - genetics Plant Proteins - metabolism Proteins Recombinant Proteins Transgenes |
title | A galactosyltransferase acting on arabinogalactan protein glycans is essential for embryo development in Arabidopsis |
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