Hmg-coA reductase gene family in cotton (Gossypium hirsutum L.): Unique structural features and differential expression of hmg2 potentially associated with synthesis of specific isoprenoids in developing embryos
As a first step towards understanding the biosynthesis of isoprenoids that accumulate in specialized pigment glands of cotton at the molecular level, two full-length genes (hmg1 and hmg2) were characterized encoding hmgcoA reductase (HMGR; EC 1.1.1.34), the enzyme that catalyzes the formation of a k...
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Veröffentlicht in: | Plant and cell physiology 1999-07, Vol.40 (7), p.750-761 |
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description | As a first step towards understanding the biosynthesis of isoprenoids that accumulate in specialized pigment glands of cotton at the molecular level, two full-length genes (hmg1 and hmg2) were characterized encoding hmgcoA reductase (HMGR; EC 1.1.1.34), the enzyme that catalyzes the formation of a key isoprenoid precursor. Cotton hmgr genes exhibited features typical of other plant genes, however, hmg2 encodes the largest of all plant HMGR enzymes described to date. HMG2 contains several novel features that may represent functional specialization of this particular HMCR isoform. Such features include a unique 42 amino acid sequence located in the region separating the N-terminal domain and C-terminal catalytic domain, as well as an N-terminal hydrophobic domain that is not found in HMG1 or other HMGR enzymes. DNA blot analysis revealed that hmg1 and hmg2 belong to small subfamilies that probably include homeologous loci in allotetraploid cotton (Gossypium hirsutum L.). Ribonuclease protection assays revealed that hmg1 and hmg2 are differentially expressed in a developmentally-and spatially-modulated manner during morphogenesis of specialized ter penoid-containing pigment glands in embryos. Induced expression of hmg2 coincided with a possible commitment to sesquiterpenoid biosynthesis in developing embryos, although other developmental processes also requiring HMGR cannot be excluded. |
doi_str_mv | 10.1093/oxfordjournals.pcp.a029602 |
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(University of California, Davis (USA)) ; Scott, H.C ; Trolinder, N.L ; Wilkins, T.A</creator><creatorcontrib>Loguercio, L.L. (University of California, Davis (USA)) ; Scott, H.C ; Trolinder, N.L ; Wilkins, T.A</creatorcontrib><description>As a first step towards understanding the biosynthesis of isoprenoids that accumulate in specialized pigment glands of cotton at the molecular level, two full-length genes (hmg1 and hmg2) were characterized encoding hmgcoA reductase (HMGR; EC 1.1.1.34), the enzyme that catalyzes the formation of a key isoprenoid precursor. Cotton hmgr genes exhibited features typical of other plant genes, however, hmg2 encodes the largest of all plant HMGR enzymes described to date. HMG2 contains several novel features that may represent functional specialization of this particular HMCR isoform. Such features include a unique 42 amino acid sequence located in the region separating the N-terminal domain and C-terminal catalytic domain, as well as an N-terminal hydrophobic domain that is not found in HMG1 or other HMGR enzymes. DNA blot analysis revealed that hmg1 and hmg2 belong to small subfamilies that probably include homeologous loci in allotetraploid cotton (Gossypium hirsutum L.). Ribonuclease protection assays revealed that hmg1 and hmg2 are differentially expressed in a developmentally-and spatially-modulated manner during morphogenesis of specialized ter penoid-containing pigment glands in embryos. Induced expression of hmg2 coincided with a possible commitment to sesquiterpenoid biosynthesis in developing embryos, although other developmental processes also requiring HMGR cannot be excluded.</description><identifier>ISSN: 0032-0781</identifier><identifier>EISSN: 1471-9053</identifier><identifier>DOI: 10.1093/oxfordjournals.pcp.a029602</identifier><identifier>PMID: 10501034</identifier><language>eng</language><publisher>Japan: Oxford University Press</publisher><subject>Base Sequence ; BIOSINTESIS ; BIOSYNTHESE ; BIOSYNTHESIS ; Cotton ; DNA Primers - genetics ; DNA, Plant - genetics ; EMBRIONES VEGETALES ; EMBRYON VEGETAL ; GENE ; Gene Expression Regulation, Developmental ; Gene Expression Regulation, Enzymologic ; Gene family ; GENES ; Genes, Plant ; Gossypium - embryology ; Gossypium - enzymology ; Gossypium - genetics ; GOSSYPIUM HIRSUTUM ; HMGR (EC 1.1.1.34) ; Hydroxymethylglutaryl CoA Reductases - genetics ; Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent ; ISOPRENOIDE ; ISOPRENOIDES ; ISOPRENOIDS ; Molecular Sequence Data ; Multigene Family ; OXIDOREDUCTASES ; OXIDORREDUCTASAS ; OXYDOREDUCTASE ; PLANT EMBRYOS ; Polyisoprenyl Phosphates - biosynthesis</subject><ispartof>Plant and cell physiology, 1999-07, Vol.40 (7), p.750-761</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-9b81d63ca4f09c6ea440f8dea26707b7429410e0b549db8f85d7372a857e92e63</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10501034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Loguercio, L.L. (University of California, Davis (USA))</creatorcontrib><creatorcontrib>Scott, H.C</creatorcontrib><creatorcontrib>Trolinder, N.L</creatorcontrib><creatorcontrib>Wilkins, T.A</creatorcontrib><title>Hmg-coA reductase gene family in cotton (Gossypium hirsutum L.): Unique structural features and differential expression of hmg2 potentially associated with synthesis of specific isoprenoids in developing embryos</title><title>Plant and cell physiology</title><addtitle>Plant Cell Physiol</addtitle><description>As a first step towards understanding the biosynthesis of isoprenoids that accumulate in specialized pigment glands of cotton at the molecular level, two full-length genes (hmg1 and hmg2) were characterized encoding hmgcoA reductase (HMGR; EC 1.1.1.34), the enzyme that catalyzes the formation of a key isoprenoid precursor. Cotton hmgr genes exhibited features typical of other plant genes, however, hmg2 encodes the largest of all plant HMGR enzymes described to date. HMG2 contains several novel features that may represent functional specialization of this particular HMCR isoform. Such features include a unique 42 amino acid sequence located in the region separating the N-terminal domain and C-terminal catalytic domain, as well as an N-terminal hydrophobic domain that is not found in HMG1 or other HMGR enzymes. DNA blot analysis revealed that hmg1 and hmg2 belong to small subfamilies that probably include homeologous loci in allotetraploid cotton (Gossypium hirsutum L.). Ribonuclease protection assays revealed that hmg1 and hmg2 are differentially expressed in a developmentally-and spatially-modulated manner during morphogenesis of specialized ter penoid-containing pigment glands in embryos. Induced expression of hmg2 coincided with a possible commitment to sesquiterpenoid biosynthesis in developing embryos, although other developmental processes also requiring HMGR cannot be excluded.</description><subject>Base Sequence</subject><subject>BIOSINTESIS</subject><subject>BIOSYNTHESE</subject><subject>BIOSYNTHESIS</subject><subject>Cotton</subject><subject>DNA Primers - genetics</subject><subject>DNA, Plant - genetics</subject><subject>EMBRIONES VEGETALES</subject><subject>EMBRYON VEGETAL</subject><subject>GENE</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Gene family</subject><subject>GENES</subject><subject>Genes, Plant</subject><subject>Gossypium - embryology</subject><subject>Gossypium - enzymology</subject><subject>Gossypium - genetics</subject><subject>GOSSYPIUM HIRSUTUM</subject><subject>HMGR (EC 1.1.1.34)</subject><subject>Hydroxymethylglutaryl CoA Reductases - genetics</subject><subject>Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent</subject><subject>ISOPRENOIDE</subject><subject>ISOPRENOIDES</subject><subject>ISOPRENOIDS</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>OXIDOREDUCTASES</subject><subject>OXIDORREDUCTASAS</subject><subject>OXYDOREDUCTASE</subject><subject>PLANT EMBRYOS</subject><subject>Polyisoprenyl Phosphates - biosynthesis</subject><issn>0032-0781</issn><issn>1471-9053</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQxiMEotvCI4AsDggOWZw4f5zeqgq60JXgQCXUi-XY412XJE49Dt19Tl4IL1khOOGLRzO_-caeL0leZXSZ0Ya9czvjvL5zkx9kh8tRjUtJ86ai-aNkkRV1lja0ZI-TBaUsT2nNs5PkFPGO0hgz-jQ5yWhJM8qKRfJz1W9S5S6IBz2pIBHIBgYgRva22xM7EOVCcAN5c-UQ96OderK1HqcQg_Xy7Tm5Gez9BASDj_2Tlx0xIGMASOSgibbGgIch2FiB3RjzaKOeM2Tbb3IyujAX4zSJ6JSVATR5sGFLcD-ELaDFA40jKGusIhZdVBmc1Xh4n4Yf0LnRDhsCfev3Dp8lT0xcDDw_3mfJzYf3Xy9X6frz1cfLi3WqipKHtGl5piumZGFooyqQRUEN1yDzqqZ1Wxd5U2QUaFsWjW654aWuWZ1LXtbQ5FCxs-T1rDt6F1eAQfQWFXSdHMBNKKJK3bCG_xfMasYaylkEz2dQ-bhtD0aM3vbS70VGxcF78a_3Inovjt7H5pfHKVPbg_6rdTY7AukMWAyw-1OX_ruo4s9Ksfp2K675dVWubnNx4F_MvJFOyI23KD59yenvw3PGfgGV4s8_</recordid><startdate>19990701</startdate><enddate>19990701</enddate><creator>Loguercio, L.L. (University of California, Davis (USA))</creator><creator>Scott, H.C</creator><creator>Trolinder, N.L</creator><creator>Wilkins, T.A</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</scope><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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19990701</creationdate><title>Hmg-coA reductase gene family in cotton (Gossypium hirsutum L.): Unique structural features and differential expression of hmg2 potentially associated with synthesis of specific isoprenoids in developing embryos</title><author>Loguercio, L.L. (University of California, Davis (USA)) ; Scott, H.C ; Trolinder, N.L ; Wilkins, T.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-9b81d63ca4f09c6ea440f8dea26707b7429410e0b549db8f85d7372a857e92e63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Base Sequence</topic><topic>BIOSINTESIS</topic><topic>BIOSYNTHESE</topic><topic>BIOSYNTHESIS</topic><topic>Cotton</topic><topic>DNA Primers - genetics</topic><topic>DNA, Plant - genetics</topic><topic>EMBRIONES VEGETALES</topic><topic>EMBRYON VEGETAL</topic><topic>GENE</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Gene family</topic><topic>GENES</topic><topic>Genes, Plant</topic><topic>Gossypium - embryology</topic><topic>Gossypium - enzymology</topic><topic>Gossypium - genetics</topic><topic>GOSSYPIUM HIRSUTUM</topic><topic>HMGR (EC 1.1.1.34)</topic><topic>Hydroxymethylglutaryl CoA Reductases - genetics</topic><topic>Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent</topic><topic>ISOPRENOIDE</topic><topic>ISOPRENOIDES</topic><topic>ISOPRENOIDS</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>OXIDOREDUCTASES</topic><topic>OXIDORREDUCTASAS</topic><topic>OXYDOREDUCTASE</topic><topic>PLANT EMBRYOS</topic><topic>Polyisoprenyl Phosphates - biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Loguercio, L.L. (University of California, Davis (USA))</creatorcontrib><creatorcontrib>Scott, H.C</creatorcontrib><creatorcontrib>Trolinder, N.L</creatorcontrib><creatorcontrib>Wilkins, T.A</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Plant and cell physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Loguercio, L.L. (University of California, Davis (USA))</au><au>Scott, H.C</au><au>Trolinder, N.L</au><au>Wilkins, T.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hmg-coA reductase gene family in cotton (Gossypium hirsutum L.): Unique structural features and differential expression of hmg2 potentially associated with synthesis of specific isoprenoids in developing embryos</atitle><jtitle>Plant and cell physiology</jtitle><addtitle>Plant Cell Physiol</addtitle><date>1999-07-01</date><risdate>1999</risdate><volume>40</volume><issue>7</issue><spage>750</spage><epage>761</epage><pages>750-761</pages><issn>0032-0781</issn><eissn>1471-9053</eissn><abstract>As a first step towards understanding the biosynthesis of isoprenoids that accumulate in specialized pigment glands of cotton at the molecular level, two full-length genes (hmg1 and hmg2) were characterized encoding hmgcoA reductase (HMGR; EC 1.1.1.34), the enzyme that catalyzes the formation of a key isoprenoid precursor. Cotton hmgr genes exhibited features typical of other plant genes, however, hmg2 encodes the largest of all plant HMGR enzymes described to date. HMG2 contains several novel features that may represent functional specialization of this particular HMCR isoform. Such features include a unique 42 amino acid sequence located in the region separating the N-terminal domain and C-terminal catalytic domain, as well as an N-terminal hydrophobic domain that is not found in HMG1 or other HMGR enzymes. DNA blot analysis revealed that hmg1 and hmg2 belong to small subfamilies that probably include homeologous loci in allotetraploid cotton (Gossypium hirsutum L.). Ribonuclease protection assays revealed that hmg1 and hmg2 are differentially expressed in a developmentally-and spatially-modulated manner during morphogenesis of specialized ter penoid-containing pigment glands in embryos. Induced expression of hmg2 coincided with a possible commitment to sesquiterpenoid biosynthesis in developing embryos, although other developmental processes also requiring HMGR cannot be excluded.</abstract><cop>Japan</cop><pub>Oxford University Press</pub><pmid>10501034</pmid><doi>10.1093/oxfordjournals.pcp.a029602</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals |
subjects | Base Sequence BIOSINTESIS BIOSYNTHESE BIOSYNTHESIS Cotton DNA Primers - genetics DNA, Plant - genetics EMBRIONES VEGETALES EMBRYON VEGETAL GENE Gene Expression Regulation, Developmental Gene Expression Regulation, Enzymologic Gene family GENES Genes, Plant Gossypium - embryology Gossypium - enzymology Gossypium - genetics GOSSYPIUM HIRSUTUM HMGR (EC 1.1.1.34) Hydroxymethylglutaryl CoA Reductases - genetics Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent ISOPRENOIDE ISOPRENOIDES ISOPRENOIDS Molecular Sequence Data Multigene Family OXIDOREDUCTASES OXIDORREDUCTASAS OXYDOREDUCTASE PLANT EMBRYOS Polyisoprenyl Phosphates - biosynthesis |
title | Hmg-coA reductase gene family in cotton (Gossypium hirsutum L.): Unique structural features and differential expression of hmg2 potentially associated with synthesis of specific isoprenoids in developing embryos |
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