A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6
Abstract Secretory and membrane proteins synthesized in the endoplasmic reticulum (ER) are folded with intramolecular disulphide bonds, viz. oxidative folding, catalysed by the protein disulphide isomerase (PDI) family proteins. Here, we identified a novel soybean PDI family protein, GmPDIL6. GmPDIL...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2020-10, Vol.168 (4), p.393-405 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Okuda, Aya Matsusaki, Motonori Masuda, Taro Morishima, Ken Sato, Nobuhiro Inoue, Rintaro Sugiyama, Masaaki Urade, Reiko |
| description | Abstract
Secretory and membrane proteins synthesized in the endoplasmic reticulum (ER) are folded with intramolecular disulphide bonds, viz. oxidative folding, catalysed by the protein disulphide isomerase (PDI) family proteins. Here, we identified a novel soybean PDI family protein, GmPDIL6. GmPDIL6 has a single thioredoxin-domain with a putative N-terminal signal peptide and an active centre (CKHC). Recombinant GmPDIL6 forms various oligomers binding iron. Oligomers with or without iron binding and monomers exhibited a dithiol oxidase activity level comparable to those of other soybean PDI family proteins. However, they displayed no disulphide reductase and extremely low oxidative refolding activity. Interestingly, GmPDIL6 was mainly expressed in the cotyledon during synthesis of seed storage proteins and GmPDIL6 mRNA was up-regulated under ER stress. GmPDIL6 may play a role in the formation of disulphide bonds in nascent proteins for oxidative folding in the ER. |
| doi_str_mv | 10.1093/jb/mvaa058 |
| format | Article |
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Secretory and membrane proteins synthesized in the endoplasmic reticulum (ER) are folded with intramolecular disulphide bonds, viz. oxidative folding, catalysed by the protein disulphide isomerase (PDI) family proteins. Here, we identified a novel soybean PDI family protein, GmPDIL6. GmPDIL6 has a single thioredoxin-domain with a putative N-terminal signal peptide and an active centre (CKHC). Recombinant GmPDIL6 forms various oligomers binding iron. Oligomers with or without iron binding and monomers exhibited a dithiol oxidase activity level comparable to those of other soybean PDI family proteins. However, they displayed no disulphide reductase and extremely low oxidative refolding activity. Interestingly, GmPDIL6 was mainly expressed in the cotyledon during synthesis of seed storage proteins and GmPDIL6 mRNA was up-regulated under ER stress. GmPDIL6 may play a role in the formation of disulphide bonds in nascent proteins for oxidative folding in the ER.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/jb/mvaa058</identifier><identifier>PMID: 32458972</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Sequence ; Cloning, Molecular - methods ; Endoplasmic Reticulum - metabolism ; Glycine max - enzymology ; Oxidation-Reduction ; Protein Disulfide-Isomerases - chemistry ; Protein Disulfide-Isomerases - genetics ; Protein Disulfide-Isomerases - metabolism ; Protein Folding ; Sequence Homology ; Toluene - analogs & derivatives ; Toluene - chemistry ; Toluene - metabolism</subject><ispartof>Journal of biochemistry (Tokyo), 2020-10, Vol.168 (4), p.393-405</ispartof><rights>The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved 2020</rights><rights>The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c393t-2390b41b7f4c734266d36c680392407d419948508629189bf2dfaaeecfd6952a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32458972$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Okuda, Aya</creatorcontrib><creatorcontrib>Matsusaki, Motonori</creatorcontrib><creatorcontrib>Masuda, Taro</creatorcontrib><creatorcontrib>Morishima, Ken</creatorcontrib><creatorcontrib>Sato, Nobuhiro</creatorcontrib><creatorcontrib>Inoue, Rintaro</creatorcontrib><creatorcontrib>Sugiyama, Masaaki</creatorcontrib><creatorcontrib>Urade, Reiko</creatorcontrib><title>A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Abstract
Secretory and membrane proteins synthesized in the endoplasmic reticulum (ER) are folded with intramolecular disulphide bonds, viz. oxidative folding, catalysed by the protein disulphide isomerase (PDI) family proteins. Here, we identified a novel soybean PDI family protein, GmPDIL6. GmPDIL6 has a single thioredoxin-domain with a putative N-terminal signal peptide and an active centre (CKHC). Recombinant GmPDIL6 forms various oligomers binding iron. Oligomers with or without iron binding and monomers exhibited a dithiol oxidase activity level comparable to those of other soybean PDI family proteins. However, they displayed no disulphide reductase and extremely low oxidative refolding activity. Interestingly, GmPDIL6 was mainly expressed in the cotyledon during synthesis of seed storage proteins and GmPDIL6 mRNA was up-regulated under ER stress. GmPDIL6 may play a role in the formation of disulphide bonds in nascent proteins for oxidative folding in the ER.</description><subject>Amino Acid Sequence</subject><subject>Cloning, Molecular - methods</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Glycine max - enzymology</subject><subject>Oxidation-Reduction</subject><subject>Protein Disulfide-Isomerases - chemistry</subject><subject>Protein Disulfide-Isomerases - genetics</subject><subject>Protein Disulfide-Isomerases - metabolism</subject><subject>Protein Folding</subject><subject>Sequence Homology</subject><subject>Toluene - analogs & derivatives</subject><subject>Toluene - chemistry</subject><subject>Toluene - metabolism</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kd1KwzAYhoMobk5PvADJiSBCXX7atPFsTJ2DgR4oeFbS_LCMtqlNO5xX4SWbsblDIRDyfQ8PvHkBuMToDiNOx6tiXK2FQEl2BIY4TVhEWIKPwRAhgiNO4o8BOPN-tX0SSk_BgJI4yXhKhuBnAmu31iX0blNoUcOmdZ22NVTW92WztEpD612lW-E1NKKy5ebANM57vT2B7pbWldB9WSU662ooZGfXttvcw6CoO2us3C9qBeVStAHQrf3eDZ2Bs-r1Yb5g5-DEiNLri_09Au9Pj2_T52jxMptPJ4tIUk67iFCOihgXqYllSmPCmKJMsgzRkBelKsacx1mCMkY4znhhiDJCaC2NYjwhgo7Azc4bwnz22nd5Zb3UZSlq7Xqfby0UpzFPA3q7Q2UbArfa5E1rK9FucozybQP5qsj3DQT4au_ti0qrA_r35QG43gGub_4T_QJvt5G2</recordid><startdate>20201001</startdate><enddate>20201001</enddate><creator>Okuda, Aya</creator><creator>Matsusaki, Motonori</creator><creator>Masuda, Taro</creator><creator>Morishima, Ken</creator><creator>Sato, Nobuhiro</creator><creator>Inoue, Rintaro</creator><creator>Sugiyama, Masaaki</creator><creator>Urade, Reiko</creator><general>Oxford University Press</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>7X8</scope></search><sort><creationdate>20201001</creationdate><title>A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6</title><author>Okuda, Aya ; Matsusaki, Motonori ; Masuda, Taro ; Morishima, Ken ; Sato, Nobuhiro ; Inoue, Rintaro ; Sugiyama, Masaaki ; Urade, Reiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-2390b41b7f4c734266d36c680392407d419948508629189bf2dfaaeecfd6952a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Amino Acid Sequence</topic><topic>Cloning, Molecular - methods</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Glycine max - enzymology</topic><topic>Oxidation-Reduction</topic><topic>Protein Disulfide-Isomerases - chemistry</topic><topic>Protein Disulfide-Isomerases - genetics</topic><topic>Protein Disulfide-Isomerases - metabolism</topic><topic>Protein Folding</topic><topic>Sequence Homology</topic><topic>Toluene - analogs & derivatives</topic><topic>Toluene - chemistry</topic><topic>Toluene - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Okuda, Aya</creatorcontrib><creatorcontrib>Matsusaki, Motonori</creatorcontrib><creatorcontrib>Masuda, Taro</creatorcontrib><creatorcontrib>Morishima, Ken</creatorcontrib><creatorcontrib>Sato, Nobuhiro</creatorcontrib><creatorcontrib>Inoue, Rintaro</creatorcontrib><creatorcontrib>Sugiyama, Masaaki</creatorcontrib><creatorcontrib>Urade, Reiko</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Okuda, Aya</au><au>Matsusaki, Motonori</au><au>Masuda, Taro</au><au>Morishima, Ken</au><au>Sato, Nobuhiro</au><au>Inoue, Rintaro</au><au>Sugiyama, Masaaki</au><au>Urade, Reiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2020-10-01</date><risdate>2020</risdate><volume>168</volume><issue>4</issue><spage>393</spage><epage>405</epage><pages>393-405</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>Abstract
Secretory and membrane proteins synthesized in the endoplasmic reticulum (ER) are folded with intramolecular disulphide bonds, viz. oxidative folding, catalysed by the protein disulphide isomerase (PDI) family proteins. Here, we identified a novel soybean PDI family protein, GmPDIL6. GmPDIL6 has a single thioredoxin-domain with a putative N-terminal signal peptide and an active centre (CKHC). Recombinant GmPDIL6 forms various oligomers binding iron. Oligomers with or without iron binding and monomers exhibited a dithiol oxidase activity level comparable to those of other soybean PDI family proteins. However, they displayed no disulphide reductase and extremely low oxidative refolding activity. Interestingly, GmPDIL6 was mainly expressed in the cotyledon during synthesis of seed storage proteins and GmPDIL6 mRNA was up-regulated under ER stress. GmPDIL6 may play a role in the formation of disulphide bonds in nascent proteins for oxidative folding in the ER.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>32458972</pmid><doi>10.1093/jb/mvaa058</doi><tpages>13</tpages></addata></record> |
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| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Cloning, Molecular - methods Endoplasmic Reticulum - metabolism Glycine max - enzymology Oxidation-Reduction Protein Disulfide-Isomerases - chemistry Protein Disulfide-Isomerases - genetics Protein Disulfide-Isomerases - metabolism Protein Folding Sequence Homology Toluene - analogs & derivatives Toluene - chemistry Toluene - metabolism |
| title | A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6 |
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