Sugar-induced increase of calcium-dependent protein kinases associated with the plasma membrane in leaf tissues of tobacco

The sugar-inducible expression of genes for sporamin and beta-amylase in leaf explants of sweet potato (Ipomoea batatas) and that of a beta-glucuronidase-fusion gene, with the promoter of the gene for beta-amylase in leaves of tobacco (Nicotiana tabacum), requires Ca2+ signaling (M. Ohto, K. Hayashi...

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Veröffentlicht in:Plant physiology (Bethesda) 1995-11, Vol.109 (3), p.973-981
Hauptverfasser: Ohto, M. (University of California, Davis, CA.), Nakamura, K
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Nakamura, K
description The sugar-inducible expression of genes for sporamin and beta-amylase in leaf explants of sweet potato (Ipomoea batatas) and that of a beta-glucuronidase-fusion gene, with the promoter of the gene for beta-amylase in leaves of tobacco (Nicotiana tabacum), requires Ca2+ signaling (M. Ohto, K. Hayashi, M. Isobe, K. Nakamura [1995] Plant J 7: 297-307), and it was inhibited by staurosporin and K252a, inhibitors of protein kinases. Autophosphorylation activities of several potential protein kinases in leaves of tobacco were significantly higher in younger leaves than in mature leaves. However, the autophosphorylation activities of these proteins in mature leaves, especially those of the major autophosphorylatable proteins with apparent molecular masses of 56 and 54 kD, increased upon treatment of leaf discs with a 0.3 M solution of sucrose, glucose, or fructose, did not increase with sorbitol or mannitol treatments, and the increase by sucrose was inhibited by cycloheximide. Autophosphorylation of the 56- and 54-kD protein in vitro was dependent on Ca2+ and inhibited by staurosporine, K-252a, and by W-7. These results suggest that they belong to the family of calcium-dependent protein kinases. They were concentrated in the plasma membrane fraction and were released from membrane vesicles by high salt or with sodium carbonate. The possible functions of these sugar-inducible calcium-dependent protein kinases associated with the plasma membrane are discussed
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(University of California, Davis, CA.) ; Nakamura, K</creator><creatorcontrib>Ohto, M. (University of California, Davis, CA.) ; Nakamura, K</creatorcontrib><description>The sugar-inducible expression of genes for sporamin and beta-amylase in leaf explants of sweet potato (Ipomoea batatas) and that of a beta-glucuronidase-fusion gene, with the promoter of the gene for beta-amylase in leaves of tobacco (Nicotiana tabacum), requires Ca2+ signaling (M. Ohto, K. Hayashi, M. Isobe, K. Nakamura [1995] Plant J 7: 297-307), and it was inhibited by staurosporin and K252a, inhibitors of protein kinases. Autophosphorylation activities of several potential protein kinases in leaves of tobacco were significantly higher in younger leaves than in mature leaves. However, the autophosphorylation activities of these proteins in mature leaves, especially those of the major autophosphorylatable proteins with apparent molecular masses of 56 and 54 kD, increased upon treatment of leaf discs with a 0.3 M solution of sucrose, glucose, or fructose, did not increase with sorbitol or mannitol treatments, and the increase by sucrose was inhibited by cycloheximide. Autophosphorylation of the 56- and 54-kD protein in vitro was dependent on Ca2+ and inhibited by staurosporine, K-252a, and by W-7. These results suggest that they belong to the family of calcium-dependent protein kinases. They were concentrated in the plasma membrane fraction and were released from membrane vesicles by high salt or with sodium carbonate. 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Psychology ; Gene expression ; HOJAS ; INHIBIDORES DE ENZIMAS ; INHIBITEUR D'ENZYME ; IPOMOEA BATATAS ; Leaves ; Messenger RNA ; Molecular and cellular biology ; Molecular genetics ; NICOTIANA TABACUM ; NUTRIENTES ; PHOSPHORYLATION ; Plant cells ; PLANTAS TRANSGENICAS ; PLANTE TRANSGENIQUE ; Plants ; Protein metabolism ; PROTEINA QUINASA ; PROTEINE KINASE ; STRUCTURE CELLULAIRE ; SUBSTANCE NUTRITIVE ; SUCRES ; Sugars ; Sweet potatoes</subject><ispartof>Plant physiology (Bethesda), 1995-11, Vol.109 (3), p.973-981</ispartof><rights>Copyright 1995 American Society of Plant Physiologists</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c486t-8dd1b40ed0a242a9f87b097ce4a4271acae20ae90ee4732d79be95a8337c9dea3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4276889$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4276889$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=2916924$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12228646$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ohto, M. (University of California, Davis, CA.)</creatorcontrib><creatorcontrib>Nakamura, K</creatorcontrib><title>Sugar-induced increase of calcium-dependent protein kinases associated with the plasma membrane in leaf tissues of tobacco</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>The sugar-inducible expression of genes for sporamin and beta-amylase in leaf explants of sweet potato (Ipomoea batatas) and that of a beta-glucuronidase-fusion gene, with the promoter of the gene for beta-amylase in leaves of tobacco (Nicotiana tabacum), requires Ca2+ signaling (M. Ohto, K. Hayashi, M. Isobe, K. Nakamura [1995] Plant J 7: 297-307), and it was inhibited by staurosporin and K252a, inhibitors of protein kinases. Autophosphorylation activities of several potential protein kinases in leaves of tobacco were significantly higher in younger leaves than in mature leaves. However, the autophosphorylation activities of these proteins in mature leaves, especially those of the major autophosphorylatable proteins with apparent molecular masses of 56 and 54 kD, increased upon treatment of leaf discs with a 0.3 M solution of sucrose, glucose, or fructose, did not increase with sorbitol or mannitol treatments, and the increase by sucrose was inhibited by cycloheximide. Autophosphorylation of the 56- and 54-kD protein in vitro was dependent on Ca2+ and inhibited by staurosporine, K-252a, and by W-7. These results suggest that they belong to the family of calcium-dependent protein kinases. They were concentrated in the plasma membrane fraction and were released from membrane vesicles by high salt or with sodium carbonate. The possible functions of these sugar-inducible calcium-dependent protein kinases associated with the plasma membrane are discussed</description><subject>Adenosine triphosphatases</subject><subject>AGE</subject><subject>AZUCARES</subject><subject>BETA AMILASA</subject><subject>BETA AMYLASE</subject><subject>Biological and medical sciences</subject><subject>CALCIO</subject><subject>CALCIUM</subject><subject>CATION</subject><subject>CATIONES</subject><subject>Cell Biology and Signal Transduction</subject><subject>Cell membranes</subject><subject>EDAD</subject><subject>ESTRUCTURA CELULAR</subject><subject>EXPRESION GENICA</subject><subject>EXPRESSION DES GENES</subject><subject>FEUILLE</subject><subject>FOSFORILACION</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>HOJAS</subject><subject>INHIBIDORES DE ENZIMAS</subject><subject>INHIBITEUR D'ENZYME</subject><subject>IPOMOEA BATATAS</subject><subject>Leaves</subject><subject>Messenger RNA</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>NICOTIANA TABACUM</subject><subject>NUTRIENTES</subject><subject>PHOSPHORYLATION</subject><subject>Plant cells</subject><subject>PLANTAS TRANSGENICAS</subject><subject>PLANTE TRANSGENIQUE</subject><subject>Plants</subject><subject>Protein metabolism</subject><subject>PROTEINA QUINASA</subject><subject>PROTEINE KINASE</subject><subject>STRUCTURE CELLULAIRE</subject><subject>SUBSTANCE NUTRITIVE</subject><subject>SUCRES</subject><subject>Sugars</subject><subject>Sweet potatoes</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNpVkb2P1DAQxSME4o6Djgoh5IKCgiz-2jgurkAnvqSTKI6rrYkz2fWRxMF2QPDXM2hXC1Qe6f3es8evqp4KvhGC6zfLshHcbtTGGnWvOhdbJWu51e396pxzmnnb2rPqUc53nHOhhH5YnQkpZdvo5rz6dbPuINVh7lePPQuzTwgZWRyYh9GHdap7XHDucS5sSbFgmNnXMBOTGeQcfYBCxh-h7FnZI1tGyBOwCacuwYyUyEaEgZWQ80oeCi6xA-_j4-rBAGPGJ8fzorp9_-7L1cf6-vOHT1dvr2uv26bUbd-LTnPsOUgtwQ6t6bg1HjVoaQR4QMkBLUfURsne2A7tFlqljLc9grqoLg-5y9pN2HvaJMHolhQmSD9dhOD-V-awd7v43YlGKGvJ_-roT_EbrVDcFLLHcaT14pqdaLdWGdMKSejrA-pTzDnhcLpFcPenLbcsNFqnHLVF-It_X_YXPtZDwMsjAJnqGOhHfcgnTlrRWKkJe37A7nKJ6STT9zRUPsnPDvIA0cEuUcLtjTWC7EL9Bk_ism4</recordid><startdate>19951101</startdate><enddate>19951101</enddate><creator>Ohto, M. (University of California, Davis, CA.)</creator><creator>Nakamura, K</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19951101</creationdate><title>Sugar-induced increase of calcium-dependent protein kinases associated with the plasma membrane in leaf tissues of tobacco</title><author>Ohto, M. (University of California, Davis, CA.) ; Nakamura, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c486t-8dd1b40ed0a242a9f87b097ce4a4271acae20ae90ee4732d79be95a8337c9dea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adenosine triphosphatases</topic><topic>AGE</topic><topic>AZUCARES</topic><topic>BETA AMILASA</topic><topic>BETA AMYLASE</topic><topic>Biological and medical sciences</topic><topic>CALCIO</topic><topic>CALCIUM</topic><topic>CATION</topic><topic>CATIONES</topic><topic>Cell Biology and Signal Transduction</topic><topic>Cell membranes</topic><topic>EDAD</topic><topic>ESTRUCTURA CELULAR</topic><topic>EXPRESION GENICA</topic><topic>EXPRESSION DES GENES</topic><topic>FEUILLE</topic><topic>FOSFORILACION</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>HOJAS</topic><topic>INHIBIDORES DE ENZIMAS</topic><topic>INHIBITEUR D'ENZYME</topic><topic>IPOMOEA BATATAS</topic><topic>Leaves</topic><topic>Messenger RNA</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>NICOTIANA TABACUM</topic><topic>NUTRIENTES</topic><topic>PHOSPHORYLATION</topic><topic>Plant cells</topic><topic>PLANTAS TRANSGENICAS</topic><topic>PLANTE TRANSGENIQUE</topic><topic>Plants</topic><topic>Protein metabolism</topic><topic>PROTEINA QUINASA</topic><topic>PROTEINE KINASE</topic><topic>STRUCTURE CELLULAIRE</topic><topic>SUBSTANCE NUTRITIVE</topic><topic>SUCRES</topic><topic>Sugars</topic><topic>Sweet potatoes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ohto, M. (University of California, Davis, CA.)</creatorcontrib><creatorcontrib>Nakamura, K</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ohto, M. 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Autophosphorylation activities of several potential protein kinases in leaves of tobacco were significantly higher in younger leaves than in mature leaves. However, the autophosphorylation activities of these proteins in mature leaves, especially those of the major autophosphorylatable proteins with apparent molecular masses of 56 and 54 kD, increased upon treatment of leaf discs with a 0.3 M solution of sucrose, glucose, or fructose, did not increase with sorbitol or mannitol treatments, and the increase by sucrose was inhibited by cycloheximide. Autophosphorylation of the 56- and 54-kD protein in vitro was dependent on Ca2+ and inhibited by staurosporine, K-252a, and by W-7. These results suggest that they belong to the family of calcium-dependent protein kinases. They were concentrated in the plasma membrane fraction and were released from membrane vesicles by high salt or with sodium carbonate. The possible functions of these sugar-inducible calcium-dependent protein kinases associated with the plasma membrane are discussed</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>12228646</pmid><doi>10.1104/pp.109.3.973</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record>
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source Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; JSTOR Archive Collection A-Z Listing; Alma/SFX Local Collection
subjects Adenosine triphosphatases
AGE
AZUCARES
BETA AMILASA
BETA AMYLASE
Biological and medical sciences
CALCIO
CALCIUM
CATION
CATIONES
Cell Biology and Signal Transduction
Cell membranes
EDAD
ESTRUCTURA CELULAR
EXPRESION GENICA
EXPRESSION DES GENES
FEUILLE
FOSFORILACION
Fundamental and applied biological sciences. Psychology
Gene expression
HOJAS
INHIBIDORES DE ENZIMAS
INHIBITEUR D'ENZYME
IPOMOEA BATATAS
Leaves
Messenger RNA
Molecular and cellular biology
Molecular genetics
NICOTIANA TABACUM
NUTRIENTES
PHOSPHORYLATION
Plant cells
PLANTAS TRANSGENICAS
PLANTE TRANSGENIQUE
Plants
Protein metabolism
PROTEINA QUINASA
PROTEINE KINASE
STRUCTURE CELLULAIRE
SUBSTANCE NUTRITIVE
SUCRES
Sugars
Sweet potatoes
title Sugar-induced increase of calcium-dependent protein kinases associated with the plasma membrane in leaf tissues of tobacco
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