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 |
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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. The possible functions of these sugar-inducible calcium-dependent protein kinases associated with the plasma membrane are discussed</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.109.3.973</identifier><identifier>PMID: 12228646</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>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</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&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. (University of California, Davis, CA.)</au><au>Nakamura, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sugar-induced increase of calcium-dependent protein kinases associated with the plasma membrane in leaf tissues of tobacco</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1995-11-01</date><risdate>1995</risdate><volume>109</volume><issue>3</issue><spage>973</spage><epage>981</epage><pages>973-981</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>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</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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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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