The subcellular localization of two isopentenyl diphosphate isomerases in rice suggests a role for the endoplasmic reticulum in isoprenoid biosynthesis
Key message Both OsIPPI1 and OsIPPI2 enzymes are found in the endoplasmic reticulum, providing novel important insights into the role of this compartment in the synthesis of MVA pathway isoprenoids. Isoprenoids are synthesized from the precursor’s isopentenyl diphosphate (IPP) and dimethylallyl diph...
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| Veröffentlicht in: | Plant cell reports 2020, Vol.39 (1), p.119-133 |
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| creator | Jin, Xin Baysal, Can Gao, Lihong Medina, Vicente Drapal, Margit Ni, Xiuzhen Sheng, Yanmin Shi, Lianxuan Capell, Teresa Fraser, Paul D. Christou, Paul Zhu, Changfu |
| description | Key message
Both OsIPPI1 and OsIPPI2 enzymes are found in the endoplasmic reticulum, providing novel important insights into the role of this compartment in the synthesis of MVA pathway isoprenoids.
Isoprenoids are synthesized from the precursor’s isopentenyl diphosphate (IPP) and dimethylallyl diphosphosphate (DMAPP), which are interconverted by the enzyme isopentenyl diphosphate isomerase (IPPI). Many plants express multiple isoforms of IPPI, the only enzyme shared by the mevalonate (MVA) and non-mevalonate (MEP) pathways, but little is known about their specific roles. Rice (
Oryza sativa
) has two IPPI isoforms (OsIPPI1 and OsIPPI2). We, therefore, carried out a comprehensive comparison of IPPI gene expression, protein localization, and isoprenoid biosynthesis in this species. We found that
OsIPPI1
mRNA was more abundant than
OsIPPI2
mRNA in all tissues, and its expression in de-etiolated leaves mirrored the accumulation of phytosterols, suggesting a key role in the synthesis of MVA pathway isoprenoids. We investigated the subcellular localization of both isoforms by constitutively expressing them as fusions with synthetic green fluorescent protein. Both proteins localized to the endoplasmic reticulum (ER) as well as peroxisomes and mitochondria, whereas only OsIPPI2 was detected in plastids, due to an N-terminal transit peptide which is not present in OsIPPI1. Despite the plastidial location of OsIPPI2, the expression of
OsIPPI2
mRNA did not mirror the accumulation of chlorophylls or carotenoids, indicating that OsIPPI2 may be a redundant component of the MEP pathway. The detection of both OsIPPI isoforms in the ER indicates that DMAPP can be synthesized de novo in this compartment. Our work shows that the ER plays an as yet unknown role in the synthesis of MVA-derived isoprenoids, with important implications for the metabolic engineering of isoprenoid biosynthesis in higher plants. |
| doi_str_mv | 10.1007/s00299-019-02479-x |
| format | Article |
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Both OsIPPI1 and OsIPPI2 enzymes are found in the endoplasmic reticulum, providing novel important insights into the role of this compartment in the synthesis of MVA pathway isoprenoids.
Isoprenoids are synthesized from the precursor’s isopentenyl diphosphate (IPP) and dimethylallyl diphosphosphate (DMAPP), which are interconverted by the enzyme isopentenyl diphosphate isomerase (IPPI). Many plants express multiple isoforms of IPPI, the only enzyme shared by the mevalonate (MVA) and non-mevalonate (MEP) pathways, but little is known about their specific roles. Rice (
Oryza sativa
) has two IPPI isoforms (OsIPPI1 and OsIPPI2). We, therefore, carried out a comprehensive comparison of IPPI gene expression, protein localization, and isoprenoid biosynthesis in this species. We found that
OsIPPI1
mRNA was more abundant than
OsIPPI2
mRNA in all tissues, and its expression in de-etiolated leaves mirrored the accumulation of phytosterols, suggesting a key role in the synthesis of MVA pathway isoprenoids. We investigated the subcellular localization of both isoforms by constitutively expressing them as fusions with synthetic green fluorescent protein. Both proteins localized to the endoplasmic reticulum (ER) as well as peroxisomes and mitochondria, whereas only OsIPPI2 was detected in plastids, due to an N-terminal transit peptide which is not present in OsIPPI1. Despite the plastidial location of OsIPPI2, the expression of
OsIPPI2
mRNA did not mirror the accumulation of chlorophylls or carotenoids, indicating that OsIPPI2 may be a redundant component of the MEP pathway. The detection of both OsIPPI isoforms in the ER indicates that DMAPP can be synthesized de novo in this compartment. Our work shows that the ER plays an as yet unknown role in the synthesis of MVA-derived isoprenoids, with important implications for the metabolic engineering of isoprenoid biosynthesis in higher plants.</description><identifier>ISSN: 0721-7714</identifier><identifier>EISSN: 1432-203X</identifier><identifier>DOI: 10.1007/s00299-019-02479-x</identifier><identifier>PMID: 31679061</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Accumulation ; Biomedical and Life Sciences ; Biosynthesis ; Biotechnology ; Carbon-Carbon Double Bond Isomerases - genetics ; Carbon-Carbon Double Bond Isomerases - metabolism ; Carotenoids ; Carotenoids - metabolism ; Cell Biology ; Chlorophyll ; Chlorophyll - metabolism ; Endoplasmic reticulum ; Endoplasmic Reticulum - enzymology ; Endoplasmic Reticulum - metabolism ; Enzymes ; Fluorescence ; Gene expression ; Gene Expression Regulation, Plant ; Green fluorescent protein ; Hemiterpenes - genetics ; Hemiterpenes - metabolism ; Isoforms ; Isopentenyl diphosphate ; Life Sciences ; Localization ; Metabolic engineering ; Mevalonate pathway ; Mevalonic acid ; Mevalonic Acid - metabolism ; Mitochondria ; Mitochondria - metabolism ; Organophosphorus Compounds - metabolism ; Original Article ; Oryza - enzymology ; Oryza - genetics ; Oryza - metabolism ; Oryza sativa ; Peroxisomes ; Peroxisomes - metabolism ; Phytosterols ; Plant Biochemistry ; Plant Leaves - metabolism ; Plant Sciences ; Plants, Genetically Modified - cytology ; Plants, Genetically Modified - genetics ; Plants, Genetically Modified - metabolism ; Plastids ; Plastids - metabolism ; Protein biosynthesis ; Proteins ; Redundant components ; Rice ; Terpenes ; Terpenes - metabolism</subject><ispartof>Plant cell reports, 2020, Vol.39 (1), p.119-133</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2019</rights><rights>Plant Cell Reports is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-cda407e6641d2c4d04feb4a878f1405be0de655f3f97b0e967c32d3e8df108573</citedby><cites>FETCH-LOGICAL-c375t-cda407e6641d2c4d04feb4a878f1405be0de655f3f97b0e967c32d3e8df108573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00299-019-02479-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00299-019-02479-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31679061$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jin, Xin</creatorcontrib><creatorcontrib>Baysal, Can</creatorcontrib><creatorcontrib>Gao, Lihong</creatorcontrib><creatorcontrib>Medina, Vicente</creatorcontrib><creatorcontrib>Drapal, Margit</creatorcontrib><creatorcontrib>Ni, Xiuzhen</creatorcontrib><creatorcontrib>Sheng, Yanmin</creatorcontrib><creatorcontrib>Shi, Lianxuan</creatorcontrib><creatorcontrib>Capell, Teresa</creatorcontrib><creatorcontrib>Fraser, Paul D.</creatorcontrib><creatorcontrib>Christou, Paul</creatorcontrib><creatorcontrib>Zhu, Changfu</creatorcontrib><title>The subcellular localization of two isopentenyl diphosphate isomerases in rice suggests a role for the endoplasmic reticulum in isoprenoid biosynthesis</title><title>Plant cell reports</title><addtitle>Plant Cell Rep</addtitle><addtitle>Plant Cell Rep</addtitle><description>Key message
Both OsIPPI1 and OsIPPI2 enzymes are found in the endoplasmic reticulum, providing novel important insights into the role of this compartment in the synthesis of MVA pathway isoprenoids.
Isoprenoids are synthesized from the precursor’s isopentenyl diphosphate (IPP) and dimethylallyl diphosphosphate (DMAPP), which are interconverted by the enzyme isopentenyl diphosphate isomerase (IPPI). Many plants express multiple isoforms of IPPI, the only enzyme shared by the mevalonate (MVA) and non-mevalonate (MEP) pathways, but little is known about their specific roles. Rice (
Oryza sativa
) has two IPPI isoforms (OsIPPI1 and OsIPPI2). We, therefore, carried out a comprehensive comparison of IPPI gene expression, protein localization, and isoprenoid biosynthesis in this species. We found that
OsIPPI1
mRNA was more abundant than
OsIPPI2
mRNA in all tissues, and its expression in de-etiolated leaves mirrored the accumulation of phytosterols, suggesting a key role in the synthesis of MVA pathway isoprenoids. We investigated the subcellular localization of both isoforms by constitutively expressing them as fusions with synthetic green fluorescent protein. Both proteins localized to the endoplasmic reticulum (ER) as well as peroxisomes and mitochondria, whereas only OsIPPI2 was detected in plastids, due to an N-terminal transit peptide which is not present in OsIPPI1. Despite the plastidial location of OsIPPI2, the expression of
OsIPPI2
mRNA did not mirror the accumulation of chlorophylls or carotenoids, indicating that OsIPPI2 may be a redundant component of the MEP pathway. The detection of both OsIPPI isoforms in the ER indicates that DMAPP can be synthesized de novo in this compartment. Our work shows that the ER plays an as yet unknown role in the synthesis of MVA-derived isoprenoids, with important implications for the metabolic engineering of isoprenoid biosynthesis in higher plants.</description><subject>Accumulation</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Biotechnology</subject><subject>Carbon-Carbon Double Bond Isomerases - genetics</subject><subject>Carbon-Carbon Double Bond Isomerases - metabolism</subject><subject>Carotenoids</subject><subject>Carotenoids - metabolism</subject><subject>Cell Biology</subject><subject>Chlorophyll</subject><subject>Chlorophyll - metabolism</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - enzymology</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Enzymes</subject><subject>Fluorescence</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Plant</subject><subject>Green fluorescent protein</subject><subject>Hemiterpenes - genetics</subject><subject>Hemiterpenes - metabolism</subject><subject>Isoforms</subject><subject>Isopentenyl diphosphate</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Metabolic engineering</subject><subject>Mevalonate pathway</subject><subject>Mevalonic acid</subject><subject>Mevalonic Acid - metabolism</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Organophosphorus Compounds - metabolism</subject><subject>Original Article</subject><subject>Oryza - enzymology</subject><subject>Oryza - genetics</subject><subject>Oryza - metabolism</subject><subject>Oryza sativa</subject><subject>Peroxisomes</subject><subject>Peroxisomes - metabolism</subject><subject>Phytosterols</subject><subject>Plant Biochemistry</subject><subject>Plant Leaves - metabolism</subject><subject>Plant Sciences</subject><subject>Plants, Genetically Modified - cytology</subject><subject>Plants, Genetically Modified - genetics</subject><subject>Plants, Genetically Modified - metabolism</subject><subject>Plastids</subject><subject>Plastids - metabolism</subject><subject>Protein biosynthesis</subject><subject>Proteins</subject><subject>Redundant components</subject><subject>Rice</subject><subject>Terpenes</subject><subject>Terpenes - metabolism</subject><issn>0721-7714</issn><issn>1432-203X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kc1u1TAQhS0EoreFF2CBLLFhE_Bf4pslqgpFqsSmSOwix57c68qxgycRvbwIr4tDCkgsWFgjeb5zZjSHkBecveGM6bfImGjbivHyhNJtdf-I7LiSohJMfnlMdkwLXmnN1Rk5R7xjrDR185ScSd7oljV8R37cHoHi0lsIYQkm05CsCf67mX2KNA10_paoxzRBnCGeAnV-OiacjmaG9X-EbBCQ-kizt6vV4QA4IzU0pwB0SJnOZQREl6ZgcPSWZpi9XcIyrqrVO0NM3tHeJzzFQqPHZ-TJYALC84d6QT6_v7q9vK5uPn34ePnuprJS13NlnVFMQ9Mo7oRVjqkBemX2ej9wxeoemIOmrgc5tLpn0DbaSuEk7N3A2b7W8oK83nynnL4uZfNu9Lgew0RIC3ZCct4KphtR0Ff_oHdpybFsVyglFK83SmyUzQkxw9BN2Y8mnzrOujW2boutK7F1v2Lr7ovo5YP10o_g_kh-51QAuQFYWvEA-e_s_9j-BJ3Np7Q</recordid><startdate>2020</startdate><enddate>2020</enddate><creator>Jin, Xin</creator><creator>Baysal, Can</creator><creator>Gao, Lihong</creator><creator>Medina, Vicente</creator><creator>Drapal, Margit</creator><creator>Ni, Xiuzhen</creator><creator>Sheng, Yanmin</creator><creator>Shi, Lianxuan</creator><creator>Capell, Teresa</creator><creator>Fraser, Paul D.</creator><creator>Christou, Paul</creator><creator>Zhu, Changfu</creator><general>Springer Berlin Heidelberg</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>7QL</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</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>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>2020</creationdate><title>The subcellular localization of two isopentenyl diphosphate isomerases in rice suggests a role for the endoplasmic reticulum in isoprenoid biosynthesis</title><author>Jin, Xin ; Baysal, Can ; Gao, Lihong ; Medina, Vicente ; Drapal, Margit ; Ni, Xiuzhen ; Sheng, Yanmin ; Shi, Lianxuan ; Capell, Teresa ; Fraser, Paul D. ; Christou, Paul ; Zhu, Changfu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-cda407e6641d2c4d04feb4a878f1405be0de655f3f97b0e967c32d3e8df108573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Accumulation</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Biotechnology</topic><topic>Carbon-Carbon Double Bond Isomerases - genetics</topic><topic>Carbon-Carbon Double Bond Isomerases - metabolism</topic><topic>Carotenoids</topic><topic>Carotenoids - metabolism</topic><topic>Cell Biology</topic><topic>Chlorophyll</topic><topic>Chlorophyll - metabolism</topic><topic>Endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - enzymology</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Enzymes</topic><topic>Fluorescence</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Plant</topic><topic>Green fluorescent protein</topic><topic>Hemiterpenes - genetics</topic><topic>Hemiterpenes - metabolism</topic><topic>Isoforms</topic><topic>Isopentenyl diphosphate</topic><topic>Life Sciences</topic><topic>Localization</topic><topic>Metabolic engineering</topic><topic>Mevalonate pathway</topic><topic>Mevalonic acid</topic><topic>Mevalonic Acid - metabolism</topic><topic>Mitochondria</topic><topic>Mitochondria - metabolism</topic><topic>Organophosphorus Compounds - metabolism</topic><topic>Original Article</topic><topic>Oryza - enzymology</topic><topic>Oryza - genetics</topic><topic>Oryza - metabolism</topic><topic>Oryza sativa</topic><topic>Peroxisomes</topic><topic>Peroxisomes - metabolism</topic><topic>Phytosterols</topic><topic>Plant Biochemistry</topic><topic>Plant Leaves - metabolism</topic><topic>Plant Sciences</topic><topic>Plants, Genetically Modified - cytology</topic><topic>Plants, Genetically Modified - genetics</topic><topic>Plants, Genetically Modified - metabolism</topic><topic>Plastids</topic><topic>Plastids - metabolism</topic><topic>Protein biosynthesis</topic><topic>Proteins</topic><topic>Redundant components</topic><topic>Rice</topic><topic>Terpenes</topic><topic>Terpenes - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jin, Xin</creatorcontrib><creatorcontrib>Baysal, Can</creatorcontrib><creatorcontrib>Gao, Lihong</creatorcontrib><creatorcontrib>Medina, Vicente</creatorcontrib><creatorcontrib>Drapal, Margit</creatorcontrib><creatorcontrib>Ni, Xiuzhen</creatorcontrib><creatorcontrib>Sheng, Yanmin</creatorcontrib><creatorcontrib>Shi, Lianxuan</creatorcontrib><creatorcontrib>Capell, Teresa</creatorcontrib><creatorcontrib>Fraser, Paul D.</creatorcontrib><creatorcontrib>Christou, Paul</creatorcontrib><creatorcontrib>Zhu, Changfu</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</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 Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</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>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Plant cell reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jin, Xin</au><au>Baysal, Can</au><au>Gao, Lihong</au><au>Medina, Vicente</au><au>Drapal, Margit</au><au>Ni, Xiuzhen</au><au>Sheng, Yanmin</au><au>Shi, Lianxuan</au><au>Capell, Teresa</au><au>Fraser, Paul D.</au><au>Christou, Paul</au><au>Zhu, Changfu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The subcellular localization of two isopentenyl diphosphate isomerases in rice suggests a role for the endoplasmic reticulum in isoprenoid biosynthesis</atitle><jtitle>Plant cell reports</jtitle><stitle>Plant Cell Rep</stitle><addtitle>Plant Cell Rep</addtitle><date>2020</date><risdate>2020</risdate><volume>39</volume><issue>1</issue><spage>119</spage><epage>133</epage><pages>119-133</pages><issn>0721-7714</issn><eissn>1432-203X</eissn><abstract>Key message
Both OsIPPI1 and OsIPPI2 enzymes are found in the endoplasmic reticulum, providing novel important insights into the role of this compartment in the synthesis of MVA pathway isoprenoids.
Isoprenoids are synthesized from the precursor’s isopentenyl diphosphate (IPP) and dimethylallyl diphosphosphate (DMAPP), which are interconverted by the enzyme isopentenyl diphosphate isomerase (IPPI). Many plants express multiple isoforms of IPPI, the only enzyme shared by the mevalonate (MVA) and non-mevalonate (MEP) pathways, but little is known about their specific roles. Rice (
Oryza sativa
) has two IPPI isoforms (OsIPPI1 and OsIPPI2). We, therefore, carried out a comprehensive comparison of IPPI gene expression, protein localization, and isoprenoid biosynthesis in this species. We found that
OsIPPI1
mRNA was more abundant than
OsIPPI2
mRNA in all tissues, and its expression in de-etiolated leaves mirrored the accumulation of phytosterols, suggesting a key role in the synthesis of MVA pathway isoprenoids. We investigated the subcellular localization of both isoforms by constitutively expressing them as fusions with synthetic green fluorescent protein. Both proteins localized to the endoplasmic reticulum (ER) as well as peroxisomes and mitochondria, whereas only OsIPPI2 was detected in plastids, due to an N-terminal transit peptide which is not present in OsIPPI1. Despite the plastidial location of OsIPPI2, the expression of
OsIPPI2
mRNA did not mirror the accumulation of chlorophylls or carotenoids, indicating that OsIPPI2 may be a redundant component of the MEP pathway. The detection of both OsIPPI isoforms in the ER indicates that DMAPP can be synthesized de novo in this compartment. Our work shows that the ER plays an as yet unknown role in the synthesis of MVA-derived isoprenoids, with important implications for the metabolic engineering of isoprenoid biosynthesis in higher plants.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>31679061</pmid><doi>10.1007/s00299-019-02479-x</doi><tpages>15</tpages></addata></record> |
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| ispartof | Plant cell reports, 2020, Vol.39 (1), p.119-133 |
| issn | 0721-7714 1432-203X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2311920762 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Accumulation Biomedical and Life Sciences Biosynthesis Biotechnology Carbon-Carbon Double Bond Isomerases - genetics Carbon-Carbon Double Bond Isomerases - metabolism Carotenoids Carotenoids - metabolism Cell Biology Chlorophyll Chlorophyll - metabolism Endoplasmic reticulum Endoplasmic Reticulum - enzymology Endoplasmic Reticulum - metabolism Enzymes Fluorescence Gene expression Gene Expression Regulation, Plant Green fluorescent protein Hemiterpenes - genetics Hemiterpenes - metabolism Isoforms Isopentenyl diphosphate Life Sciences Localization Metabolic engineering Mevalonate pathway Mevalonic acid Mevalonic Acid - metabolism Mitochondria Mitochondria - metabolism Organophosphorus Compounds - metabolism Original Article Oryza - enzymology Oryza - genetics Oryza - metabolism Oryza sativa Peroxisomes Peroxisomes - metabolism Phytosterols Plant Biochemistry Plant Leaves - metabolism Plant Sciences Plants, Genetically Modified - cytology Plants, Genetically Modified - genetics Plants, Genetically Modified - metabolism Plastids Plastids - metabolism Protein biosynthesis Proteins Redundant components Rice Terpenes Terpenes - metabolism |
| title | The subcellular localization of two isopentenyl diphosphate isomerases in rice suggests a role for the endoplasmic reticulum in isoprenoid biosynthesis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T09%3A36%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20subcellular%20localization%20of%20two%20isopentenyl%20diphosphate%20isomerases%20in%20rice%20suggests%20a%20role%20for%20the%20endoplasmic%20reticulum%20in%20isoprenoid%20biosynthesis&rft.jtitle=Plant%20cell%20reports&rft.au=Jin,%20Xin&rft.date=2020&rft.volume=39&rft.issue=1&rft.spage=119&rft.epage=133&rft.pages=119-133&rft.issn=0721-7714&rft.eissn=1432-203X&rft_id=info:doi/10.1007/s00299-019-02479-x&rft_dat=%3Cproquest_cross%3E2311920762%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2342415762&rft_id=info:pmid/31679061&rfr_iscdi=true |