Analysis of bean (Phaseolus vulgaris L.) proteins affected by copper stress
The effect of excess copper on the expression of soluble proteins in 10-day old Phaseolus vulgaris seedlings was studied with two-dimensional electrophoresis and mass spectrometry, to find sensitive biochemical markers of exposure. Despite major differences in root Cu contents, both 15 and 50μM Cu t...
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Veröffentlicht in: | Journal of plant physiology 2005-04, Vol.162 (4), p.383-392 |
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creator | Cuypers, Ann Koistinen, Kaisa M Kokko, Harri Kärenlampi, Sirpa Auriola, Seppo Vangronsveld, Jaco |
description | The effect of excess copper on the expression of soluble proteins in 10-day old Phaseolus vulgaris seedlings was studied with two-dimensional electrophoresis and mass spectrometry, to find sensitive biochemical markers of exposure. Despite major differences in root Cu contents, both 15 and 50μM Cu treatments resulted in equal enhancements of Cu in the primary leaves.
Three proteins, apparently reacting in a dose-dependent manner to Cu exposure, were identified from roots. The levels of an intracellular pathogenesis-related protein and a newly identified protein homologous to PvPR1, PvPR2, were increased with increasing Cu concentration. The level of a newly identified PR-10 protein decreased in a dose-dependent manner.
No significant difference was observed in the leaf protein pattern between controls and 15μM Cu-treated plants. However, at 50μM Cu exposure, the appearance of PvPR1 and a homologue of Arabidopsis thaliana thylakoid lumenal 17.4kDa protein was observed. Another protein slightly enhanced by Cu treatment had sequence homology to a mitochondrial precursor of glycine cleavage system H protein of Flaveria pringlei. |
doi_str_mv | 10.1016/j.jplph.2004.07.018 |
format | Article |
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Three proteins, apparently reacting in a dose-dependent manner to Cu exposure, were identified from roots. The levels of an intracellular pathogenesis-related protein and a newly identified protein homologous to PvPR1, PvPR2, were increased with increasing Cu concentration. The level of a newly identified PR-10 protein decreased in a dose-dependent manner.
No significant difference was observed in the leaf protein pattern between controls and 15μM Cu-treated plants. However, at 50μM Cu exposure, the appearance of PvPR1 and a homologue of Arabidopsis thaliana thylakoid lumenal 17.4kDa protein was observed. Another protein slightly enhanced by Cu treatment had sequence homology to a mitochondrial precursor of glycine cleavage system H protein of Flaveria pringlei.</description><identifier>ISSN: 0176-1617</identifier><identifier>EISSN: 1618-1328</identifier><identifier>DOI: 10.1016/j.jplph.2004.07.018</identifier><identifier>PMID: 15900880</identifier><identifier>CODEN: JPPHEY</identifier><language>eng</language><publisher>Jena: Elsevier GmbH</publisher><subject>Amino Acid Sequence ; amino acid sequences ; beans ; Biological and medical sciences ; copper ; Copper - toxicity ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Plant - drug effects ; Mass spectrometry ; Molecular Sequence Data ; Pathogenesis-related (PR) protein ; Phaseolus - drug effects ; Phaseolus - metabolism ; Phaseolus vulgaris ; Physiological diseases. Varia ; Phytopathology. Animal pests. Plant and forest protection ; Plant Leaves - metabolism ; plant proteins ; Plant Proteins - metabolism ; Plant Roots - metabolism ; plant stress ; polyacrylamide gel electrophoresis ; PR-10 ; roots ; seedlings ; Sequence Homology, Amino Acid ; spectral analysis ; Two-dimensional electrophoresis ; uptake mechanisms</subject><ispartof>Journal of plant physiology, 2005-04, Vol.162 (4), p.383-392</ispartof><rights>2004 Elsevier GmbH</rights><rights>2005 INIST-CNRS</rights><rights>Copyright Urban & Fischer Verlag Apr 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-5ca64504ac4297e10a6be5768e7ec072cfe23aa2fd980f5ee2985867a7fe876c3</citedby><cites>FETCH-LOGICAL-c504t-5ca64504ac4297e10a6be5768e7ec072cfe23aa2fd980f5ee2985867a7fe876c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0176161704002007$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16721073$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15900880$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cuypers, Ann</creatorcontrib><creatorcontrib>Koistinen, Kaisa M</creatorcontrib><creatorcontrib>Kokko, Harri</creatorcontrib><creatorcontrib>Kärenlampi, Sirpa</creatorcontrib><creatorcontrib>Auriola, Seppo</creatorcontrib><creatorcontrib>Vangronsveld, Jaco</creatorcontrib><title>Analysis of bean (Phaseolus vulgaris L.) proteins affected by copper stress</title><title>Journal of plant physiology</title><addtitle>J Plant Physiol</addtitle><description>The effect of excess copper on the expression of soluble proteins in 10-day old Phaseolus vulgaris seedlings was studied with two-dimensional electrophoresis and mass spectrometry, to find sensitive biochemical markers of exposure. Despite major differences in root Cu contents, both 15 and 50μM Cu treatments resulted in equal enhancements of Cu in the primary leaves.
Three proteins, apparently reacting in a dose-dependent manner to Cu exposure, were identified from roots. The levels of an intracellular pathogenesis-related protein and a newly identified protein homologous to PvPR1, PvPR2, were increased with increasing Cu concentration. The level of a newly identified PR-10 protein decreased in a dose-dependent manner.
No significant difference was observed in the leaf protein pattern between controls and 15μM Cu-treated plants. However, at 50μM Cu exposure, the appearance of PvPR1 and a homologue of Arabidopsis thaliana thylakoid lumenal 17.4kDa protein was observed. Another protein slightly enhanced by Cu treatment had sequence homology to a mitochondrial precursor of glycine cleavage system H protein of Flaveria pringlei.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>beans</subject><subject>Biological and medical sciences</subject><subject>copper</subject><subject>Copper - toxicity</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Plant - drug effects</subject><subject>Mass spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Pathogenesis-related (PR) protein</subject><subject>Phaseolus - drug effects</subject><subject>Phaseolus - metabolism</subject><subject>Phaseolus vulgaris</subject><subject>Physiological diseases. Varia</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Plant Leaves - metabolism</subject><subject>plant proteins</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Roots - metabolism</subject><subject>plant stress</subject><subject>polyacrylamide gel electrophoresis</subject><subject>PR-10</subject><subject>roots</subject><subject>seedlings</subject><subject>Sequence Homology, Amino Acid</subject><subject>spectral analysis</subject><subject>Two-dimensional electrophoresis</subject><subject>uptake mechanisms</subject><issn>0176-1617</issn><issn>1618-1328</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kE1r3DAQhkVpaLZpf0GhNYFCc7A7km1JPvQQQr_oQgttzmJWHiU2ju1q7MD--yjdhdx6kjR65mXmEeKNhEKC1B_7op-H-bZQAFUBpgBpn4mN1NLmslT2udiANDpPBXMqXjL3kN61LV-IU1k3ANbCRvy4HHHYc8fZFLId4Zh9-HWLTNOwcna_DjcY09-2uMjmOC3UjZxhCOQXarPdPvPTPFPMeInE_EqcBByYXh_PM3H95fOfq2_59ufX71eX29zXUC157VFX6Ya-Uo0hCah3VBttyZAHo3wgVSKq0DYWQk2kGltbbdAEskb78kycH3LTSH9X4sX10xrTHuwUaGsbAypB5QHycWKOFNwcuzuMeyfBPfpzvfvnzz36c2Bc8pe63h6j190dtU89R2EJeH8EkD0OIeLoO37itFESTJm4dwcu4OTwJkl0178VyBIkQNlAlYhPB4KSqvuOomPf0eip7WLy69qp---oD7Nml1M</recordid><startdate>20050401</startdate><enddate>20050401</enddate><creator>Cuypers, Ann</creator><creator>Koistinen, Kaisa M</creator><creator>Kokko, Harri</creator><creator>Kärenlampi, Sirpa</creator><creator>Auriola, Seppo</creator><creator>Vangronsveld, Jaco</creator><general>Elsevier GmbH</general><general>Elsevier</general><general>Elsevier Science Ltd</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>3V.</scope><scope>7QP</scope><scope>7SS</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>S0X</scope></search><sort><creationdate>20050401</creationdate><title>Analysis of bean (Phaseolus vulgaris L.) proteins affected by copper stress</title><author>Cuypers, Ann ; Koistinen, Kaisa M ; Kokko, Harri ; Kärenlampi, Sirpa ; Auriola, Seppo ; Vangronsveld, Jaco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-5ca64504ac4297e10a6be5768e7ec072cfe23aa2fd980f5ee2985867a7fe876c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>beans</topic><topic>Biological and medical sciences</topic><topic>copper</topic><topic>Copper - toxicity</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Plant - drug effects</topic><topic>Mass spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Pathogenesis-related (PR) protein</topic><topic>Phaseolus - drug effects</topic><topic>Phaseolus - metabolism</topic><topic>Phaseolus vulgaris</topic><topic>Physiological diseases. Varia</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Plant Leaves - metabolism</topic><topic>plant proteins</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Roots - metabolism</topic><topic>plant stress</topic><topic>polyacrylamide gel electrophoresis</topic><topic>PR-10</topic><topic>roots</topic><topic>seedlings</topic><topic>Sequence Homology, Amino Acid</topic><topic>spectral analysis</topic><topic>Two-dimensional electrophoresis</topic><topic>uptake mechanisms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cuypers, Ann</creatorcontrib><creatorcontrib>Koistinen, Kaisa M</creatorcontrib><creatorcontrib>Kokko, Harri</creatorcontrib><creatorcontrib>Kärenlampi, Sirpa</creatorcontrib><creatorcontrib>Auriola, Seppo</creatorcontrib><creatorcontrib>Vangronsveld, Jaco</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE 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Phaseolus vulgaris seedlings was studied with two-dimensional electrophoresis and mass spectrometry, to find sensitive biochemical markers of exposure. Despite major differences in root Cu contents, both 15 and 50μM Cu treatments resulted in equal enhancements of Cu in the primary leaves.
Three proteins, apparently reacting in a dose-dependent manner to Cu exposure, were identified from roots. The levels of an intracellular pathogenesis-related protein and a newly identified protein homologous to PvPR1, PvPR2, were increased with increasing Cu concentration. The level of a newly identified PR-10 protein decreased in a dose-dependent manner.
No significant difference was observed in the leaf protein pattern between controls and 15μM Cu-treated plants. However, at 50μM Cu exposure, the appearance of PvPR1 and a homologue of Arabidopsis thaliana thylakoid lumenal 17.4kDa protein was observed. Another protein slightly enhanced by Cu treatment had sequence homology to a mitochondrial precursor of glycine cleavage system H protein of Flaveria pringlei.</abstract><cop>Jena</cop><pub>Elsevier GmbH</pub><pmid>15900880</pmid><doi>10.1016/j.jplph.2004.07.018</doi><tpages>10</tpages></addata></record> |
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subjects | Amino Acid Sequence amino acid sequences beans Biological and medical sciences copper Copper - toxicity Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Plant - drug effects Mass spectrometry Molecular Sequence Data Pathogenesis-related (PR) protein Phaseolus - drug effects Phaseolus - metabolism Phaseolus vulgaris Physiological diseases. Varia Phytopathology. Animal pests. Plant and forest protection Plant Leaves - metabolism plant proteins Plant Proteins - metabolism Plant Roots - metabolism plant stress polyacrylamide gel electrophoresis PR-10 roots seedlings Sequence Homology, Amino Acid spectral analysis Two-dimensional electrophoresis uptake mechanisms |
title | Analysis of bean (Phaseolus vulgaris L.) proteins affected by copper stress |
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