Purification and characterization of Arabidopsis thaliana oligosaccharyltransferase complexes from the native host: a protein super‐expression system for structural studies
Summary The oligosaccharyltransferase (OT) complex catalyzes N‐glycosylation of nascent secretory polypeptides in the lumen of the endoplasmic reticulum. Despite their importance, little is known about the structure and function of plant OT complexes, mainly due to lack of efficient recombinant prot...
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| Veröffentlicht in: | The Plant journal : for cell and molecular biology 2018-04, Vol.94 (1), p.131-145 |
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| creator | Jeong, In Sil Lee, Sangmin Bonkhofer, Florian Tolley, Jordan Fukudome, Akihito Nagashima, Yukihiro May, Kimberly Rips, Stephan Lee, Sang Y. Gallois, Patrick Russell, William K. Jung, Hyun Suk Schaewen, Antje Koiwa, Hisashi |
| description | Summary
The oligosaccharyltransferase (OT) complex catalyzes N‐glycosylation of nascent secretory polypeptides in the lumen of the endoplasmic reticulum. Despite their importance, little is known about the structure and function of plant OT complexes, mainly due to lack of efficient recombinant protein production systems suitable for studies on large plant protein complexes. Here, we purified Arabidopsis OT complexes using the tandem affinity‐tagged OT subunit STAUROSPORINE AND TEMPERATURE SENSITIVE3a (STT3a) expressed by an Arabidopsis protein super‐expression platform. Mass‐spectrometry analysis of the purified complexes identified three essential OT subunits, OLIGOSACCHARYLTRANSFERASE1 (OST1), HAPLESS6 (HAP6), DEFECTIVE GLYCOSYLATION1 (DGL1), and a number of ribosomal subunits. Transmission‐electron microscopy showed that STT3a becomes incorporated into OT–ribosome super‐complexes formed in vivo, demonstrating that this expression/purification platform is suitable for analysis of large protein complexes. Pairwise in planta interaction analyses of individual OT subunits demonstrated that all subunits identified in animal OT complexes are conserved in Arabidopsis and physically interact with STT3a. Genetic analysis of newly established OT subunit mutants for OST1 and DEFENDER AGAINST APOTOTIC DEATH (DAD) family genes revealed that OST1 and DAD1/2 subunits are essential for the plant life cycle. However, mutations in these individual isoforms produced much milder growth/underglycosylation phenotypes than previously reported for mutations in DGL1, OST3/6 and STT3a.
Significance Statement
A protein super‐expression system was established that is suitable for studying higher‐order structure and function of protein super‐complexes using Arabidopsis cell cultures. The system enabled the production and isolation of authentic oligosaccharyltransferase (OT) complexes assembled on a recombinant STT3a subunit, leading to identification and characterization of OT subunits and solving the three‐dimensional structure of plant OT–ribosome complexes. |
| doi_str_mv | 10.1111/tpj.13847 |
| format | Article |
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The oligosaccharyltransferase (OT) complex catalyzes N‐glycosylation of nascent secretory polypeptides in the lumen of the endoplasmic reticulum. Despite their importance, little is known about the structure and function of plant OT complexes, mainly due to lack of efficient recombinant protein production systems suitable for studies on large plant protein complexes. Here, we purified Arabidopsis OT complexes using the tandem affinity‐tagged OT subunit STAUROSPORINE AND TEMPERATURE SENSITIVE3a (STT3a) expressed by an Arabidopsis protein super‐expression platform. Mass‐spectrometry analysis of the purified complexes identified three essential OT subunits, OLIGOSACCHARYLTRANSFERASE1 (OST1), HAPLESS6 (HAP6), DEFECTIVE GLYCOSYLATION1 (DGL1), and a number of ribosomal subunits. Transmission‐electron microscopy showed that STT3a becomes incorporated into OT–ribosome super‐complexes formed in vivo, demonstrating that this expression/purification platform is suitable for analysis of large protein complexes. Pairwise in planta interaction analyses of individual OT subunits demonstrated that all subunits identified in animal OT complexes are conserved in Arabidopsis and physically interact with STT3a. Genetic analysis of newly established OT subunit mutants for OST1 and DEFENDER AGAINST APOTOTIC DEATH (DAD) family genes revealed that OST1 and DAD1/2 subunits are essential for the plant life cycle. However, mutations in these individual isoforms produced much milder growth/underglycosylation phenotypes than previously reported for mutations in DGL1, OST3/6 and STT3a.
Significance Statement
A protein super‐expression system was established that is suitable for studying higher‐order structure and function of protein super‐complexes using Arabidopsis cell cultures. The system enabled the production and isolation of authentic oligosaccharyltransferase (OT) complexes assembled on a recombinant STT3a subunit, leading to identification and characterization of OT subunits and solving the three‐dimensional structure of plant OT–ribosome complexes.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1111/tpj.13847</identifier><identifier>PMID: 29385647</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Arabidopsis ; Arabidopsis thaliana ; Electron microscopy ; Endoplasmic reticulum ; Genetic analysis ; Glycosylation ; Isoforms ; Life cycle engineering ; Life cycles ; Mutants ; Mutation ; Oligosaccharyltransferase ; oligosaccharyltransferase complex ; Polypeptides ; protein N‐glycosylation ; Protein purification ; Proteins ; Purification ; Ribosomal subunits ; ribosome ; Spectrometry ; Staurosporine ; Structure-function relationships ; tandem affinity purification ; transmission electron microscopy</subject><ispartof>The Plant journal : for cell and molecular biology, 2018-04, Vol.94 (1), p.131-145</ispartof><rights>2018 The Authors The Plant Journal © 2018 John Wiley & Sons Ltd</rights><rights>2018 The Authors The Plant Journal © 2018 John Wiley & Sons Ltd.</rights><rights>Copyright © 2018 John Wiley & Sons Ltd and the Society for Experimental Biology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4547-d50530b0b595aff956d7c5077e3611d4cab037656f02d710271808c14cf051cf3</citedby><cites>FETCH-LOGICAL-c4547-d50530b0b595aff956d7c5077e3611d4cab037656f02d710271808c14cf051cf3</cites><orcidid>0000-0002-6305-2807</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.13847$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Ftpj.13847$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29385647$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jeong, In Sil</creatorcontrib><creatorcontrib>Lee, Sangmin</creatorcontrib><creatorcontrib>Bonkhofer, Florian</creatorcontrib><creatorcontrib>Tolley, Jordan</creatorcontrib><creatorcontrib>Fukudome, Akihito</creatorcontrib><creatorcontrib>Nagashima, Yukihiro</creatorcontrib><creatorcontrib>May, Kimberly</creatorcontrib><creatorcontrib>Rips, Stephan</creatorcontrib><creatorcontrib>Lee, Sang Y.</creatorcontrib><creatorcontrib>Gallois, Patrick</creatorcontrib><creatorcontrib>Russell, William K.</creatorcontrib><creatorcontrib>Jung, Hyun Suk</creatorcontrib><creatorcontrib>Schaewen, Antje</creatorcontrib><creatorcontrib>Koiwa, Hisashi</creatorcontrib><title>Purification and characterization of Arabidopsis thaliana oligosaccharyltransferase complexes from the native host: a protein super‐expression system for structural studies</title><title>The Plant journal : for cell and molecular biology</title><addtitle>Plant J</addtitle><description>Summary
The oligosaccharyltransferase (OT) complex catalyzes N‐glycosylation of nascent secretory polypeptides in the lumen of the endoplasmic reticulum. Despite their importance, little is known about the structure and function of plant OT complexes, mainly due to lack of efficient recombinant protein production systems suitable for studies on large plant protein complexes. Here, we purified Arabidopsis OT complexes using the tandem affinity‐tagged OT subunit STAUROSPORINE AND TEMPERATURE SENSITIVE3a (STT3a) expressed by an Arabidopsis protein super‐expression platform. Mass‐spectrometry analysis of the purified complexes identified three essential OT subunits, OLIGOSACCHARYLTRANSFERASE1 (OST1), HAPLESS6 (HAP6), DEFECTIVE GLYCOSYLATION1 (DGL1), and a number of ribosomal subunits. Transmission‐electron microscopy showed that STT3a becomes incorporated into OT–ribosome super‐complexes formed in vivo, demonstrating that this expression/purification platform is suitable for analysis of large protein complexes. Pairwise in planta interaction analyses of individual OT subunits demonstrated that all subunits identified in animal OT complexes are conserved in Arabidopsis and physically interact with STT3a. Genetic analysis of newly established OT subunit mutants for OST1 and DEFENDER AGAINST APOTOTIC DEATH (DAD) family genes revealed that OST1 and DAD1/2 subunits are essential for the plant life cycle. However, mutations in these individual isoforms produced much milder growth/underglycosylation phenotypes than previously reported for mutations in DGL1, OST3/6 and STT3a.
Significance Statement
A protein super‐expression system was established that is suitable for studying higher‐order structure and function of protein super‐complexes using Arabidopsis cell cultures. The system enabled the production and isolation of authentic oligosaccharyltransferase (OT) complexes assembled on a recombinant STT3a subunit, leading to identification and characterization of OT subunits and solving the three‐dimensional structure of plant OT–ribosome complexes.</description><subject>Arabidopsis</subject><subject>Arabidopsis thaliana</subject><subject>Electron microscopy</subject><subject>Endoplasmic reticulum</subject><subject>Genetic analysis</subject><subject>Glycosylation</subject><subject>Isoforms</subject><subject>Life cycle engineering</subject><subject>Life cycles</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Oligosaccharyltransferase</subject><subject>oligosaccharyltransferase complex</subject><subject>Polypeptides</subject><subject>protein N‐glycosylation</subject><subject>Protein purification</subject><subject>Proteins</subject><subject>Purification</subject><subject>Ribosomal subunits</subject><subject>ribosome</subject><subject>Spectrometry</subject><subject>Staurosporine</subject><subject>Structure-function relationships</subject><subject>tandem affinity purification</subject><subject>transmission electron microscopy</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp1kU9u1TAQhy0Eoo_CggsgS2xgkdaOYzthV1X8VSW6KBK7yHHGPD8lcfA4pY8VR-AkHIqT4EcKCyS8sWV9881ofoQ85uyE53Oa5t0JF3Wl75ANF0oWgouPd8mGNYoVuuLlEXmAuGOMa6Gq--SobEQtVaU35MflEr3z1iQfJmqmntqticYmiP7r-hkcPYum832Y0SNNWzN4MxkaBv8poLGHgv2QopnQQTQI1IZxHuAGkLoYxlwBdMqua6DbgOkFNXSOIYGfKC4zxJ_fvsPNHAHx0A73mGCkLkSKKS42LdEM-bn0HvAhuefMgPDo9j4mH169vDp_U1y8f_32_OyisJWsdNFLJgXrWCcbaZxrpOq1lUxrEIrzvrKmY0IrqRwre81ZqXnNassr65jk1olj8mz15kE_L4CpHT1aGAYzQViw5U0jRF0qoTP69B90F5Y45enaMi9cNSWXPFPPV8rGgBjBtXP0Y15cy1l7CLHNIba_Q8zsk1vj0o3Q_yX_pJaB0xX44gfY_9_UXl2-W5W_AMGSrAQ</recordid><startdate>201804</startdate><enddate>201804</enddate><creator>Jeong, In Sil</creator><creator>Lee, Sangmin</creator><creator>Bonkhofer, Florian</creator><creator>Tolley, Jordan</creator><creator>Fukudome, Akihito</creator><creator>Nagashima, Yukihiro</creator><creator>May, Kimberly</creator><creator>Rips, Stephan</creator><creator>Lee, Sang Y.</creator><creator>Gallois, Patrick</creator><creator>Russell, William K.</creator><creator>Jung, Hyun Suk</creator><creator>Schaewen, Antje</creator><creator>Koiwa, Hisashi</creator><general>Blackwell Publishing Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</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><orcidid>https://orcid.org/0000-0002-6305-2807</orcidid></search><sort><creationdate>201804</creationdate><title>Purification and characterization of Arabidopsis thaliana oligosaccharyltransferase complexes from the native host: a protein super‐expression system for structural studies</title><author>Jeong, In Sil ; Lee, Sangmin ; Bonkhofer, Florian ; Tolley, Jordan ; Fukudome, Akihito ; Nagashima, Yukihiro ; May, Kimberly ; Rips, Stephan ; Lee, Sang Y. ; Gallois, Patrick ; Russell, William K. ; Jung, Hyun Suk ; Schaewen, Antje ; Koiwa, Hisashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4547-d50530b0b595aff956d7c5077e3611d4cab037656f02d710271808c14cf051cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Arabidopsis</topic><topic>Arabidopsis thaliana</topic><topic>Electron microscopy</topic><topic>Endoplasmic reticulum</topic><topic>Genetic analysis</topic><topic>Glycosylation</topic><topic>Isoforms</topic><topic>Life cycle engineering</topic><topic>Life cycles</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Oligosaccharyltransferase</topic><topic>oligosaccharyltransferase complex</topic><topic>Polypeptides</topic><topic>protein N‐glycosylation</topic><topic>Protein purification</topic><topic>Proteins</topic><topic>Purification</topic><topic>Ribosomal subunits</topic><topic>ribosome</topic><topic>Spectrometry</topic><topic>Staurosporine</topic><topic>Structure-function relationships</topic><topic>tandem affinity purification</topic><topic>transmission electron microscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jeong, In Sil</creatorcontrib><creatorcontrib>Lee, Sangmin</creatorcontrib><creatorcontrib>Bonkhofer, Florian</creatorcontrib><creatorcontrib>Tolley, Jordan</creatorcontrib><creatorcontrib>Fukudome, Akihito</creatorcontrib><creatorcontrib>Nagashima, Yukihiro</creatorcontrib><creatorcontrib>May, Kimberly</creatorcontrib><creatorcontrib>Rips, Stephan</creatorcontrib><creatorcontrib>Lee, Sang Y.</creatorcontrib><creatorcontrib>Gallois, Patrick</creatorcontrib><creatorcontrib>Russell, William K.</creatorcontrib><creatorcontrib>Jung, Hyun Suk</creatorcontrib><creatorcontrib>Schaewen, Antje</creatorcontrib><creatorcontrib>Koiwa, Hisashi</creatorcontrib><collection>PubMed</collection><collection>CrossRef</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><jtitle>The Plant journal : for cell and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jeong, In Sil</au><au>Lee, Sangmin</au><au>Bonkhofer, Florian</au><au>Tolley, Jordan</au><au>Fukudome, Akihito</au><au>Nagashima, Yukihiro</au><au>May, Kimberly</au><au>Rips, Stephan</au><au>Lee, Sang Y.</au><au>Gallois, Patrick</au><au>Russell, William K.</au><au>Jung, Hyun Suk</au><au>Schaewen, Antje</au><au>Koiwa, Hisashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of Arabidopsis thaliana oligosaccharyltransferase complexes from the native host: a protein super‐expression system for structural studies</atitle><jtitle>The Plant journal : for cell and molecular biology</jtitle><addtitle>Plant J</addtitle><date>2018-04</date><risdate>2018</risdate><volume>94</volume><issue>1</issue><spage>131</spage><epage>145</epage><pages>131-145</pages><issn>0960-7412</issn><eissn>1365-313X</eissn><abstract>Summary
The oligosaccharyltransferase (OT) complex catalyzes N‐glycosylation of nascent secretory polypeptides in the lumen of the endoplasmic reticulum. Despite their importance, little is known about the structure and function of plant OT complexes, mainly due to lack of efficient recombinant protein production systems suitable for studies on large plant protein complexes. Here, we purified Arabidopsis OT complexes using the tandem affinity‐tagged OT subunit STAUROSPORINE AND TEMPERATURE SENSITIVE3a (STT3a) expressed by an Arabidopsis protein super‐expression platform. Mass‐spectrometry analysis of the purified complexes identified three essential OT subunits, OLIGOSACCHARYLTRANSFERASE1 (OST1), HAPLESS6 (HAP6), DEFECTIVE GLYCOSYLATION1 (DGL1), and a number of ribosomal subunits. Transmission‐electron microscopy showed that STT3a becomes incorporated into OT–ribosome super‐complexes formed in vivo, demonstrating that this expression/purification platform is suitable for analysis of large protein complexes. Pairwise in planta interaction analyses of individual OT subunits demonstrated that all subunits identified in animal OT complexes are conserved in Arabidopsis and physically interact with STT3a. Genetic analysis of newly established OT subunit mutants for OST1 and DEFENDER AGAINST APOTOTIC DEATH (DAD) family genes revealed that OST1 and DAD1/2 subunits are essential for the plant life cycle. However, mutations in these individual isoforms produced much milder growth/underglycosylation phenotypes than previously reported for mutations in DGL1, OST3/6 and STT3a.
Significance Statement
A protein super‐expression system was established that is suitable for studying higher‐order structure and function of protein super‐complexes using Arabidopsis cell cultures. The system enabled the production and isolation of authentic oligosaccharyltransferase (OT) complexes assembled on a recombinant STT3a subunit, leading to identification and characterization of OT subunits and solving the three‐dimensional structure of plant OT–ribosome complexes.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>29385647</pmid><doi>10.1111/tpj.13847</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0002-6305-2807</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Arabidopsis Arabidopsis thaliana Electron microscopy Endoplasmic reticulum Genetic analysis Glycosylation Isoforms Life cycle engineering Life cycles Mutants Mutation Oligosaccharyltransferase oligosaccharyltransferase complex Polypeptides protein N‐glycosylation Protein purification Proteins Purification Ribosomal subunits ribosome Spectrometry Staurosporine Structure-function relationships tandem affinity purification transmission electron microscopy |
| title | Purification and characterization of Arabidopsis thaliana oligosaccharyltransferase complexes from the native host: a protein super‐expression system for structural studies |
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