Expression and localization of calcium-dependent protein kinase isoforms in chickpea
Calcium-dependent protein kinases (CPKs) play important roles in multiple signal transduction pathways but the precise role of individual CPK is largely unknown. We isolated two cDNAs encoding two CPK isoforms ( Cicer arietinum CPKs—CaCPK1 and CaCPK2) of chickpea. Their expression in various organs...
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| Veröffentlicht in: | Journal of plant physiology 2006-11, Vol.163 (11), p.1135-1149 |
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| creator | Syam Prakash, S.R. Jayabaskaran, Chelliah |
| description | Calcium-dependent protein kinases (CPKs) play important roles in multiple signal transduction pathways but the precise role of individual CPK is largely unknown. We isolated two cDNAs encoding two CPK isoforms (
Cicer arietinum CPKs—CaCPK1 and CaCPK2) of chickpea. Their expression in various organs and in response to various phytohormones, and dehydration, high salt stress and fungal spore in excised leaves as well as localization in leaf and stem tissues were analyzed in this study. CaCPK1 protein and its activity were ubiquitous in all tissues examined. In contrast, CaCPK2 transcript, CaCPK2 protein and its activity were almost undetectable in flowers and fruits. Both CaCPK1 and CaCPK2 transcripts and proteins were abundant in roots but in minor quantities in leaves and stems. Of the three phytohormones tested, viz. indole-3-acetic acid (IAA), gibberellin (GA
3) and benzyladenine (BA), only BA increased both CaCPK1 and CaCPK2 transcripts, proteins and their activities. GA
3 induced accumulation of CaCPK2 transcript and protein but CaCPK1 remained unaffected. The expression of CaCPK1 and CaCPK2 in leaves was enhanced in response to high salt stress. Treatments with
Aspergillus sp. spores increased expression of CaCPK1 in chickpea leaf tissue but had no effect on CaCPK2. Excised leaves subjected to dehydration showed increase in CaCPK2 expression but not in CaCPK1. Both isoforms were located in the plasma membrane (PM) and chloroplast membrane of leaf mesophyll cells as well as in the PM of stem xylem parenchyma cells. These results suggest specific roles for CaCPK isoforms in phytohormone/defense/stress signaling pathways. |
| doi_str_mv | 10.1016/j.jplph.2006.04.002 |
| format | Article |
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Cicer arietinum CPKs—CaCPK1 and CaCPK2) of chickpea. Their expression in various organs and in response to various phytohormones, and dehydration, high salt stress and fungal spore in excised leaves as well as localization in leaf and stem tissues were analyzed in this study. CaCPK1 protein and its activity were ubiquitous in all tissues examined. In contrast, CaCPK2 transcript, CaCPK2 protein and its activity were almost undetectable in flowers and fruits. Both CaCPK1 and CaCPK2 transcripts and proteins were abundant in roots but in minor quantities in leaves and stems. Of the three phytohormones tested, viz. indole-3-acetic acid (IAA), gibberellin (GA
3) and benzyladenine (BA), only BA increased both CaCPK1 and CaCPK2 transcripts, proteins and their activities. GA
3 induced accumulation of CaCPK2 transcript and protein but CaCPK1 remained unaffected. The expression of CaCPK1 and CaCPK2 in leaves was enhanced in response to high salt stress. Treatments with
Aspergillus sp. spores increased expression of CaCPK1 in chickpea leaf tissue but had no effect on CaCPK2. Excised leaves subjected to dehydration showed increase in CaCPK2 expression but not in CaCPK1. Both isoforms were located in the plasma membrane (PM) and chloroplast membrane of leaf mesophyll cells as well as in the PM of stem xylem parenchyma cells. These results suggest specific roles for CaCPK isoforms in phytohormone/defense/stress signaling pathways.</description><identifier>ISSN: 0176-1617</identifier><identifier>EISSN: 1618-1328</identifier><identifier>DOI: 10.1016/j.jplph.2006.04.002</identifier><identifier>PMID: 16716453</identifier><identifier>CODEN: JPPHEY</identifier><language>eng</language><publisher>Jena: Elsevier GmbH</publisher><subject>Aminobutyrates - metabolism ; Aspergillus ; benzyladenine ; Biological and medical sciences ; calcium-dependent protein kinase ; Calcium-dependent protein kinase isoforms ; chickpeas ; Chloroplast membrane ; chloroplasts ; Chloroplasts - enzymology ; Cicer - chemistry ; Cicer - enzymology ; Cicer - genetics ; Cicer arietinum ; complementary DNA ; desiccation (plant physiology) ; enzyme activity ; Enzymes ; Fundamental and applied biological sciences. Psychology ; fungal spores ; gene expression regulation ; Gene Expression Regulation, Plant ; gibberellins ; Gibberellins - metabolism ; Immunolocalization ; indole acetic acid ; Indoleacetic Acids - metabolism ; Isoenzymes - analysis ; Isoenzymes - genetics ; isozymes ; membrane proteins ; messenger RNA ; Metabolism ; molecular cloning ; Molecular Sequence Data ; physiological response ; plant biochemistry ; plant genetics ; plant growth substances ; Plant physiology and development ; Plant Proteins - analysis ; Plant Proteins - genetics ; plant response ; protein content ; protein kinases ; Protein Kinases - analysis ; Protein Kinases - genetics ; Real-time quantitative PCR ; salt stress ; seedlings ; Seedlings - chemistry ; signal transduction ; Stresses ; tissue distribution</subject><ispartof>Journal of plant physiology, 2006-11, Vol.163 (11), p.1135-1149</ispartof><rights>2006 Elsevier GmbH</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c477t-7b0d285c865c553efe0f3d77a04df9f79631a9c02182959ffdb295c24f6bf30d3</citedby><cites>FETCH-LOGICAL-c477t-7b0d285c865c553efe0f3d77a04df9f79631a9c02182959ffdb295c24f6bf30d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jplph.2006.04.002$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27928,27929,45999</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18255463$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16716453$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Syam Prakash, S.R.</creatorcontrib><creatorcontrib>Jayabaskaran, Chelliah</creatorcontrib><title>Expression and localization of calcium-dependent protein kinase isoforms in chickpea</title><title>Journal of plant physiology</title><addtitle>J Plant Physiol</addtitle><description>Calcium-dependent protein kinases (CPKs) play important roles in multiple signal transduction pathways but the precise role of individual CPK is largely unknown. We isolated two cDNAs encoding two CPK isoforms (
Cicer arietinum CPKs—CaCPK1 and CaCPK2) of chickpea. Their expression in various organs and in response to various phytohormones, and dehydration, high salt stress and fungal spore in excised leaves as well as localization in leaf and stem tissues were analyzed in this study. CaCPK1 protein and its activity were ubiquitous in all tissues examined. In contrast, CaCPK2 transcript, CaCPK2 protein and its activity were almost undetectable in flowers and fruits. Both CaCPK1 and CaCPK2 transcripts and proteins were abundant in roots but in minor quantities in leaves and stems. Of the three phytohormones tested, viz. indole-3-acetic acid (IAA), gibberellin (GA
3) and benzyladenine (BA), only BA increased both CaCPK1 and CaCPK2 transcripts, proteins and their activities. GA
3 induced accumulation of CaCPK2 transcript and protein but CaCPK1 remained unaffected. The expression of CaCPK1 and CaCPK2 in leaves was enhanced in response to high salt stress. Treatments with
Aspergillus sp. spores increased expression of CaCPK1 in chickpea leaf tissue but had no effect on CaCPK2. Excised leaves subjected to dehydration showed increase in CaCPK2 expression but not in CaCPK1. Both isoforms were located in the plasma membrane (PM) and chloroplast membrane of leaf mesophyll cells as well as in the PM of stem xylem parenchyma cells. These results suggest specific roles for CaCPK isoforms in phytohormone/defense/stress signaling pathways.</description><subject>Aminobutyrates - metabolism</subject><subject>Aspergillus</subject><subject>benzyladenine</subject><subject>Biological and medical sciences</subject><subject>calcium-dependent protein kinase</subject><subject>Calcium-dependent protein kinase isoforms</subject><subject>chickpeas</subject><subject>Chloroplast membrane</subject><subject>chloroplasts</subject><subject>Chloroplasts - enzymology</subject><subject>Cicer - chemistry</subject><subject>Cicer - enzymology</subject><subject>Cicer - genetics</subject><subject>Cicer arietinum</subject><subject>complementary DNA</subject><subject>desiccation (plant physiology)</subject><subject>enzyme activity</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>fungal spores</subject><subject>gene expression regulation</subject><subject>Gene Expression Regulation, Plant</subject><subject>gibberellins</subject><subject>Gibberellins - metabolism</subject><subject>Immunolocalization</subject><subject>indole acetic acid</subject><subject>Indoleacetic Acids - metabolism</subject><subject>Isoenzymes - analysis</subject><subject>Isoenzymes - genetics</subject><subject>isozymes</subject><subject>membrane proteins</subject><subject>messenger RNA</subject><subject>Metabolism</subject><subject>molecular cloning</subject><subject>Molecular Sequence Data</subject><subject>physiological response</subject><subject>plant biochemistry</subject><subject>plant genetics</subject><subject>plant growth substances</subject><subject>Plant physiology and development</subject><subject>Plant Proteins - analysis</subject><subject>Plant Proteins - genetics</subject><subject>plant response</subject><subject>protein content</subject><subject>protein kinases</subject><subject>Protein Kinases - analysis</subject><subject>Protein Kinases - genetics</subject><subject>Real-time quantitative PCR</subject><subject>salt stress</subject><subject>seedlings</subject><subject>Seedlings - chemistry</subject><subject>signal transduction</subject><subject>Stresses</subject><subject>tissue distribution</subject><issn>0176-1617</issn><issn>1618-1328</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi0EosvCL0CCXOCWMLZjOzlwQFX5kCpxoD1bXntMvU3sYGcR8Ovxsiv1xmk0r553NHoIeUmho0Dlu323X6blrmMAsoO-A2CPyIZKOrSUs-Ex2QBVsq2BuiDPStlD3cXAn5ILKhWVveAbcnP1a8lYSkixMdE1U7JmCn_MegySb-pmw2FuHS4YHca1WXJaMcTmPkRTsAkl-ZTn0tTI3gV7v6B5Tp54MxV8cZ5bcvvx6ubyc3v99dOXyw_Xre2VWlu1A8cGYQcprBAcPYLnTikDvfOjV6Pk1IwWGB3YKEbv3a5Oy3ovd56D41vy9nS3_vTjgGXVcygWp8lETIei5TD2A5NQQX4CbU6lZPR6yWE2-bemoI8y9V7_k6mPMjX0usqsrVfn84fdjO6hc7ZXgTdnwJQqymcTbSgP3MCE6OWRe33ivEnafM-Vuf3GgHIApSSvyJa8PxFYdf0MmHWxAaNFFzLaVbsU_vvqX_-TnaY</recordid><startdate>20061101</startdate><enddate>20061101</enddate><creator>Syam Prakash, S.R.</creator><creator>Jayabaskaran, Chelliah</creator><general>Elsevier GmbH</general><general>Elsevier</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></search><sort><creationdate>20061101</creationdate><title>Expression and localization of calcium-dependent protein kinase isoforms in chickpea</title><author>Syam Prakash, S.R. ; Jayabaskaran, Chelliah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-7b0d285c865c553efe0f3d77a04df9f79631a9c02182959ffdb295c24f6bf30d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Aminobutyrates - metabolism</topic><topic>Aspergillus</topic><topic>benzyladenine</topic><topic>Biological and medical sciences</topic><topic>calcium-dependent protein kinase</topic><topic>Calcium-dependent protein kinase isoforms</topic><topic>chickpeas</topic><topic>Chloroplast membrane</topic><topic>chloroplasts</topic><topic>Chloroplasts - enzymology</topic><topic>Cicer - chemistry</topic><topic>Cicer - enzymology</topic><topic>Cicer - genetics</topic><topic>Cicer arietinum</topic><topic>complementary DNA</topic><topic>desiccation (plant physiology)</topic><topic>enzyme activity</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>fungal spores</topic><topic>gene expression regulation</topic><topic>Gene Expression Regulation, Plant</topic><topic>gibberellins</topic><topic>Gibberellins - metabolism</topic><topic>Immunolocalization</topic><topic>indole acetic acid</topic><topic>Indoleacetic Acids - metabolism</topic><topic>Isoenzymes - analysis</topic><topic>Isoenzymes - genetics</topic><topic>isozymes</topic><topic>membrane proteins</topic><topic>messenger RNA</topic><topic>Metabolism</topic><topic>molecular cloning</topic><topic>Molecular Sequence Data</topic><topic>physiological response</topic><topic>plant biochemistry</topic><topic>plant genetics</topic><topic>plant growth substances</topic><topic>Plant physiology and development</topic><topic>Plant Proteins - analysis</topic><topic>Plant Proteins - genetics</topic><topic>plant response</topic><topic>protein content</topic><topic>protein kinases</topic><topic>Protein Kinases - analysis</topic><topic>Protein Kinases - genetics</topic><topic>Real-time quantitative PCR</topic><topic>salt stress</topic><topic>seedlings</topic><topic>Seedlings - chemistry</topic><topic>signal transduction</topic><topic>Stresses</topic><topic>tissue distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Syam Prakash, S.R.</creatorcontrib><creatorcontrib>Jayabaskaran, Chelliah</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><jtitle>Journal of plant physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Syam Prakash, S.R.</au><au>Jayabaskaran, Chelliah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and localization of calcium-dependent protein kinase isoforms in chickpea</atitle><jtitle>Journal of plant physiology</jtitle><addtitle>J Plant Physiol</addtitle><date>2006-11-01</date><risdate>2006</risdate><volume>163</volume><issue>11</issue><spage>1135</spage><epage>1149</epage><pages>1135-1149</pages><issn>0176-1617</issn><eissn>1618-1328</eissn><coden>JPPHEY</coden><abstract>Calcium-dependent protein kinases (CPKs) play important roles in multiple signal transduction pathways but the precise role of individual CPK is largely unknown. We isolated two cDNAs encoding two CPK isoforms (
Cicer arietinum CPKs—CaCPK1 and CaCPK2) of chickpea. Their expression in various organs and in response to various phytohormones, and dehydration, high salt stress and fungal spore in excised leaves as well as localization in leaf and stem tissues were analyzed in this study. CaCPK1 protein and its activity were ubiquitous in all tissues examined. In contrast, CaCPK2 transcript, CaCPK2 protein and its activity were almost undetectable in flowers and fruits. Both CaCPK1 and CaCPK2 transcripts and proteins were abundant in roots but in minor quantities in leaves and stems. Of the three phytohormones tested, viz. indole-3-acetic acid (IAA), gibberellin (GA
3) and benzyladenine (BA), only BA increased both CaCPK1 and CaCPK2 transcripts, proteins and their activities. GA
3 induced accumulation of CaCPK2 transcript and protein but CaCPK1 remained unaffected. The expression of CaCPK1 and CaCPK2 in leaves was enhanced in response to high salt stress. Treatments with
Aspergillus sp. spores increased expression of CaCPK1 in chickpea leaf tissue but had no effect on CaCPK2. Excised leaves subjected to dehydration showed increase in CaCPK2 expression but not in CaCPK1. Both isoforms were located in the plasma membrane (PM) and chloroplast membrane of leaf mesophyll cells as well as in the PM of stem xylem parenchyma cells. These results suggest specific roles for CaCPK isoforms in phytohormone/defense/stress signaling pathways.</abstract><cop>Jena</cop><pub>Elsevier GmbH</pub><pmid>16716453</pmid><doi>10.1016/j.jplph.2006.04.002</doi><tpages>15</tpages></addata></record> |
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| subjects | Aminobutyrates - metabolism Aspergillus benzyladenine Biological and medical sciences calcium-dependent protein kinase Calcium-dependent protein kinase isoforms chickpeas Chloroplast membrane chloroplasts Chloroplasts - enzymology Cicer - chemistry Cicer - enzymology Cicer - genetics Cicer arietinum complementary DNA desiccation (plant physiology) enzyme activity Enzymes Fundamental and applied biological sciences. Psychology fungal spores gene expression regulation Gene Expression Regulation, Plant gibberellins Gibberellins - metabolism Immunolocalization indole acetic acid Indoleacetic Acids - metabolism Isoenzymes - analysis Isoenzymes - genetics isozymes membrane proteins messenger RNA Metabolism molecular cloning Molecular Sequence Data physiological response plant biochemistry plant genetics plant growth substances Plant physiology and development Plant Proteins - analysis Plant Proteins - genetics plant response protein content protein kinases Protein Kinases - analysis Protein Kinases - genetics Real-time quantitative PCR salt stress seedlings Seedlings - chemistry signal transduction Stresses tissue distribution |
| title | Expression and localization of calcium-dependent protein kinase isoforms in chickpea |
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