Four 9-kDa proteins excreted by somatic embryos of grapevine are isoforms of lipid-transfer proteins
Four 9-kDa small extracellular proteins produced by embryogenic cultures in the absence of auxin have been purified from the extracellular medium of grapevine somatic embryo cultures through cation-exchange chromatography and hydrophobic-interaction chromatography. The partial amino-acid sequences r...
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Veröffentlicht in: | European Journal of Biochemistry 1993-11, Vol.217 (3), p.885-889 |
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container_title | European Journal of Biochemistry |
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creator | Coutos-Thevenot, P Jouenne, T Maes, O Guerbette, F Grosbois, M Le Caer, J.P Boulay, M Deloire, A Kader, J.C Guern, J |
description | Four 9-kDa small extracellular proteins produced by embryogenic cultures in the absence of auxin have been purified from the extracellular medium of grapevine somatic embryo cultures through cation-exchange chromatography and hydrophobic-interaction chromatography. The partial amino-acid sequences reflect high similarities between the four proteins as well as with the sequences established for carrot, spinach, millet and maize nonspecific lipid-transfer proteins. All these sequences show conservation of three cysteines at positions 4, 14 and 30-32, as well as glycine, valine, tyrosine and lysine residues at positions 5, 7, 17 and 37, respectively. In-vitro lipid-transfer assays reveal that the four proteins catalyze the transfer of phosphatidylcholine from liposomes towards mitochondria with an efficiency similar or higher than that of a purified maize lipid-transfer protein. |
doi_str_mv | 10.1111/j.1432-1033.1993.tb18317.x |
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The partial amino-acid sequences reflect high similarities between the four proteins as well as with the sequences established for carrot, spinach, millet and maize nonspecific lipid-transfer proteins. All these sequences show conservation of three cysteines at positions 4, 14 and 30-32, as well as glycine, valine, tyrosine and lysine residues at positions 5, 7, 17 and 37, respectively. In-vitro lipid-transfer assays reveal that the four proteins catalyze the transfer of phosphatidylcholine from liposomes towards mitochondria with an efficiency similar or higher than that of a purified maize lipid-transfer protein.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>EISSN: 1432-1327</identifier><identifier>DOI: 10.1111/j.1432-1033.1993.tb18317.x</identifier><identifier>PMID: 8223644</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Analytical, structural and metabolic biochemistry ; Antigens, Plant ; Binding and carrier proteins ; Biological and medical sciences ; Carrier Proteins - chemistry ; Carrier Proteins - isolation & purification ; Cells, Cultured ; Chromatography, Ion Exchange ; comparisons ; Electrophoresis, Polyacrylamide Gel ; Fruit - chemistry ; Fundamental and applied biological sciences. Psychology ; genbank ; Life Sciences ; Molecular Sequence Data ; plant proteins ; Plant Proteins - chemistry ; Plant Proteins - isolation & purification ; protein secretion ; Proteins ; Seeds - chemistry ; Sequence Homology, Amino Acid ; somatic embryogenesis ; Vitis ; Vitis cinerea var. helleri ; Vitis vinifera</subject><ispartof>European Journal of Biochemistry, 1993-11, Vol.217 (3), p.885-889</ispartof><rights>1994 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4245-dc67d7423d5d4a5598f3cc8cf4a230ef0c850a4fcbf38077f9e2bdde397ff0ed3</citedby><cites>FETCH-LOGICAL-c4245-dc67d7423d5d4a5598f3cc8cf4a230ef0c850a4fcbf38077f9e2bdde397ff0ed3</cites><orcidid>0000-0003-0994-9944 ; 0000-0001-9509-6866</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27922,27923</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3829675$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8223644$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02328595$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Coutos-Thevenot, P</creatorcontrib><creatorcontrib>Jouenne, T</creatorcontrib><creatorcontrib>Maes, O</creatorcontrib><creatorcontrib>Guerbette, F</creatorcontrib><creatorcontrib>Grosbois, M</creatorcontrib><creatorcontrib>Le Caer, J.P</creatorcontrib><creatorcontrib>Boulay, M</creatorcontrib><creatorcontrib>Deloire, A</creatorcontrib><creatorcontrib>Kader, J.C</creatorcontrib><creatorcontrib>Guern, J</creatorcontrib><title>Four 9-kDa proteins excreted by somatic embryos of grapevine are isoforms of lipid-transfer proteins</title><title>European Journal of Biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Four 9-kDa small extracellular proteins produced by embryogenic cultures in the absence of auxin have been purified from the extracellular medium of grapevine somatic embryo cultures through cation-exchange chromatography and hydrophobic-interaction chromatography. The partial amino-acid sequences reflect high similarities between the four proteins as well as with the sequences established for carrot, spinach, millet and maize nonspecific lipid-transfer proteins. All these sequences show conservation of three cysteines at positions 4, 14 and 30-32, as well as glycine, valine, tyrosine and lysine residues at positions 5, 7, 17 and 37, respectively. In-vitro lipid-transfer assays reveal that the four proteins catalyze the transfer of phosphatidylcholine from liposomes towards mitochondria with an efficiency similar or higher than that of a purified maize lipid-transfer protein.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Antigens, Plant</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Cells, Cultured</subject><subject>Chromatography, Ion Exchange</subject><subject>comparisons</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fruit - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genbank</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>plant proteins</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - isolation & purification</subject><subject>protein secretion</subject><subject>Proteins</subject><subject>Seeds - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><subject>somatic embryogenesis</subject><subject>Vitis</subject><subject>Vitis cinerea var. helleri</subject><subject>Vitis vinifera</subject><issn>0014-2956</issn><issn>1432-1033</issn><issn>1432-1327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVUk2P0zAUtBBoKYWfgLAQQuKQ4K8kNhe0LFsWqRKHZc-W44_FJam7drq0_x6HRLnzLpbezJv3NGMA3mJU4lwfdyVmlBQYUVpiIWg5tJhT3JSnJ2C1QE_BCiHMCiKq-jl4kdIOIVSLurkAF5wQWjO2AmYTjhGK4vdXBQ8xDNbvE7QnHe1gDWzPMIVeDV5D27fxHBIMDt5HdbCPfm-hihb6FFyI_T-k8wdviiGqfXI2LoIvwTOnumRfze8a3G2uf17dFNsf375fXW4LzQirCqPrxjSMUFMZpqpKcEe15toxRSiyDmleIcWcbh3lqGmcsKQ1xlLROIesoWvwYdL9pTp5iL5X8SyD8vLmcivHHiKU8EpUjzhz30_cfOTD0aZB9j5p23Vqb8MxyaZGhJNs4xp8mog6hpSidYsyRnKMQ-7k6LkcPZdjHHKOQ57y8Ot5y7HtrVlGZ_8z_m7GVdKqc9k57dNCo5zkvKpM-zzR_vjOnv_jALm5_nLL-ajwZlJwKkh1H_OSu1uCMM0_hHPCBP0L4JGxVw</recordid><startdate>199311</startdate><enddate>199311</enddate><creator>Coutos-Thevenot, P</creator><creator>Jouenne, T</creator><creator>Maes, O</creator><creator>Guerbette, F</creator><creator>Grosbois, M</creator><creator>Le Caer, J.P</creator><creator>Boulay, M</creator><creator>Deloire, A</creator><creator>Kader, J.C</creator><creator>Guern, J</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Wiley</general><scope>FBQ</scope><scope>IQODW</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>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-0994-9944</orcidid><orcidid>https://orcid.org/0000-0001-9509-6866</orcidid></search><sort><creationdate>199311</creationdate><title>Four 9-kDa proteins excreted by somatic embryos of grapevine are isoforms of lipid-transfer proteins</title><author>Coutos-Thevenot, P ; Jouenne, T ; Maes, O ; Guerbette, F ; Grosbois, M ; Le Caer, J.P ; Boulay, M ; Deloire, A ; Kader, J.C ; Guern, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4245-dc67d7423d5d4a5598f3cc8cf4a230ef0c850a4fcbf38077f9e2bdde397ff0ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Antigens, Plant</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Cells, Cultured</topic><topic>Chromatography, Ion Exchange</topic><topic>comparisons</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fruit - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genbank</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>plant proteins</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - isolation & purification</topic><topic>protein secretion</topic><topic>Proteins</topic><topic>Seeds - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><topic>somatic embryogenesis</topic><topic>Vitis</topic><topic>Vitis cinerea var. helleri</topic><topic>Vitis vinifera</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Coutos-Thevenot, P</creatorcontrib><creatorcontrib>Jouenne, T</creatorcontrib><creatorcontrib>Maes, O</creatorcontrib><creatorcontrib>Guerbette, F</creatorcontrib><creatorcontrib>Grosbois, M</creatorcontrib><creatorcontrib>Le Caer, J.P</creatorcontrib><creatorcontrib>Boulay, M</creatorcontrib><creatorcontrib>Deloire, A</creatorcontrib><creatorcontrib>Kader, J.C</creatorcontrib><creatorcontrib>Guern, J</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><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><collection>Hyper Article en Ligne (HAL)</collection><jtitle>European Journal of Biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Coutos-Thevenot, P</au><au>Jouenne, T</au><au>Maes, O</au><au>Guerbette, F</au><au>Grosbois, M</au><au>Le Caer, J.P</au><au>Boulay, M</au><au>Deloire, A</au><au>Kader, J.C</au><au>Guern, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Four 9-kDa proteins excreted by somatic embryos of grapevine are isoforms of lipid-transfer proteins</atitle><jtitle>European Journal of Biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1993-11</date><risdate>1993</risdate><volume>217</volume><issue>3</issue><spage>885</spage><epage>889</epage><pages>885-889</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><eissn>1432-1327</eissn><coden>EJBCAI</coden><abstract>Four 9-kDa small extracellular proteins produced by embryogenic cultures in the absence of auxin have been purified from the extracellular medium of grapevine somatic embryo cultures through cation-exchange chromatography and hydrophobic-interaction chromatography. The partial amino-acid sequences reflect high similarities between the four proteins as well as with the sequences established for carrot, spinach, millet and maize nonspecific lipid-transfer proteins. All these sequences show conservation of three cysteines at positions 4, 14 and 30-32, as well as glycine, valine, tyrosine and lysine residues at positions 5, 7, 17 and 37, respectively. In-vitro lipid-transfer assays reveal that the four proteins catalyze the transfer of phosphatidylcholine from liposomes towards mitochondria with an efficiency similar or higher than that of a purified maize lipid-transfer protein.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8223644</pmid><doi>10.1111/j.1432-1033.1993.tb18317.x</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0003-0994-9944</orcidid><orcidid>https://orcid.org/0000-0001-9509-6866</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence amino acid sequences Analytical, structural and metabolic biochemistry Antigens, Plant Binding and carrier proteins Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - isolation & purification Cells, Cultured Chromatography, Ion Exchange comparisons Electrophoresis, Polyacrylamide Gel Fruit - chemistry Fundamental and applied biological sciences. Psychology genbank Life Sciences Molecular Sequence Data plant proteins Plant Proteins - chemistry Plant Proteins - isolation & purification protein secretion Proteins Seeds - chemistry Sequence Homology, Amino Acid somatic embryogenesis Vitis Vitis cinerea var. helleri Vitis vinifera |
title | Four 9-kDa proteins excreted by somatic embryos of grapevine are isoforms of lipid-transfer proteins |
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