Tr-cp 14 cysteine protease in white clover (Trifolium repens) is localized to the endoplasmic reticulum and is associated with programmed cell death during development of tracheary elements
Cysteine proteases are known to be associated with programmed cell death, developmental senescence and some types of pathogen and stress-induced responses. In the present study, we have characterized the cysteine protease Tr-cp 14 in white clover (Trifolium repens). Tr-cp 14 belongs to the C1A famil...
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| Veröffentlicht in: | Protoplasma 2013-04, Vol.250 (2), p.623-629 |
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| creator | Mulisch, Maria Asp, Torben Krupinska, Karin Hollmann, Julien Holm, Preben Bach |
| description | Cysteine proteases are known to be associated with programmed cell death, developmental senescence and some types of pathogen and stress-induced responses. In the present study, we have characterized the cysteine protease Tr-cp 14 in white clover (Trifolium repens). Tr-cp 14 belongs to the C1A family of cysteine proteases with homology to XCP1 and XCP2 from Arabidopsis thaliana and p48h-17 from Zinnia elegans, which previously have been reported to be associated with tracheary element differentiation. The proform as well as the processed form of the protein was detected in petioles, flowers and leaves, but the processed form was more abundant in leaves and petioles than in flowers. The Tr-cp 14 protein was localized to differentiating tracheary elements within the xylem, indicating that the cysteine protease is involved in protein re-mobilization during tracheary element differentiation. Immunogold studies suggest that the protease prior to the burst of the vacuole was associated to the ER cisternae. After disruption of the tonoplast, it was found in the cytoplasm, and, in later stages, associated with disintegrating material dispersed throughout the cell. |
| doi_str_mv | 10.1007/s00709-012-0427-1 |
| format | Article |
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In the present study, we have characterized the cysteine protease Tr-cp 14 in white clover (Trifolium repens). Tr-cp 14 belongs to the C1A family of cysteine proteases with homology to XCP1 and XCP2 from Arabidopsis thaliana and p48h-17 from Zinnia elegans, which previously have been reported to be associated with tracheary element differentiation. The proform as well as the processed form of the protein was detected in petioles, flowers and leaves, but the processed form was more abundant in leaves and petioles than in flowers. The Tr-cp 14 protein was localized to differentiating tracheary elements within the xylem, indicating that the cysteine protease is involved in protein re-mobilization during tracheary element differentiation. Immunogold studies suggest that the protease prior to the burst of the vacuole was associated to the ER cisternae. After disruption of the tonoplast, it was found in the cytoplasm, and, in later stages, associated with disintegrating material dispersed throughout the cell.</description><identifier>ISSN: 0033-183X</identifier><identifier>EISSN: 1615-6102</identifier><identifier>DOI: 10.1007/s00709-012-0427-1</identifier><identifier>PMID: 22707085</identifier><language>eng</language><publisher>Vienna: Springer-Verlag</publisher><subject>apoptosis ; Arabidopsis thaliana ; Biomedical and Life Sciences ; Cell Biology ; Cysteine Proteases - genetics ; Cysteine Proteases - metabolism ; cysteine proteinases ; endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; flowers ; Flowers - enzymology ; Flowers - metabolism ; Life Sciences ; pathogens ; petioles ; Plant Leaves - enzymology ; Plant Leaves - metabolism ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Plant Sciences ; senescence ; Short Communication ; tonoplast ; tracheary elements ; Trifolium - cytology ; Trifolium - enzymology ; Trifolium repens ; vacuoles ; Zinnia violacea ; Zoology</subject><ispartof>Protoplasma, 2013-04, Vol.250 (2), p.623-629</ispartof><rights>Springer-Verlag 2012</rights><rights>Springer-Verlag Wien 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c396t-a5fd31b31710c70e66a66d33403f7127b20e466696c1e25ccadc59882d9dacfe3</citedby><cites>FETCH-LOGICAL-c396t-a5fd31b31710c70e66a66d33403f7127b20e466696c1e25ccadc59882d9dacfe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00709-012-0427-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00709-012-0427-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,782,786,27931,27932,41495,42564,51326</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22707085$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mulisch, Maria</creatorcontrib><creatorcontrib>Asp, Torben</creatorcontrib><creatorcontrib>Krupinska, Karin</creatorcontrib><creatorcontrib>Hollmann, Julien</creatorcontrib><creatorcontrib>Holm, Preben Bach</creatorcontrib><title>Tr-cp 14 cysteine protease in white clover (Trifolium repens) is localized to the endoplasmic reticulum and is associated with programmed cell death during development of tracheary elements</title><title>Protoplasma</title><addtitle>Protoplasma</addtitle><addtitle>Protoplasma</addtitle><description>Cysteine proteases are known to be associated with programmed cell death, developmental senescence and some types of pathogen and stress-induced responses. In the present study, we have characterized the cysteine protease Tr-cp 14 in white clover (Trifolium repens). Tr-cp 14 belongs to the C1A family of cysteine proteases with homology to XCP1 and XCP2 from Arabidopsis thaliana and p48h-17 from Zinnia elegans, which previously have been reported to be associated with tracheary element differentiation. The proform as well as the processed form of the protein was detected in petioles, flowers and leaves, but the processed form was more abundant in leaves and petioles than in flowers. The Tr-cp 14 protein was localized to differentiating tracheary elements within the xylem, indicating that the cysteine protease is involved in protein re-mobilization during tracheary element differentiation. Immunogold studies suggest that the protease prior to the burst of the vacuole was associated to the ER cisternae. After disruption of the tonoplast, it was found in the cytoplasm, and, in later stages, associated with disintegrating material dispersed throughout the cell.</description><subject>apoptosis</subject><subject>Arabidopsis thaliana</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Cysteine Proteases - genetics</subject><subject>Cysteine Proteases - metabolism</subject><subject>cysteine proteinases</subject><subject>endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>flowers</subject><subject>Flowers - enzymology</subject><subject>Flowers - metabolism</subject><subject>Life Sciences</subject><subject>pathogens</subject><subject>petioles</subject><subject>Plant Leaves - enzymology</subject><subject>Plant Leaves - metabolism</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Sciences</subject><subject>senescence</subject><subject>Short Communication</subject><subject>tonoplast</subject><subject>tracheary elements</subject><subject>Trifolium - cytology</subject><subject>Trifolium - enzymology</subject><subject>Trifolium repens</subject><subject>vacuoles</subject><subject>Zinnia violacea</subject><subject>Zoology</subject><issn>0033-183X</issn><issn>1615-6102</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kU1v1DAQhi0EosvCD-AClriUQ2DGTpzkiCq-pEoc2ErcIq8z2XXlxMF2WpX_xn_D0RaEOHCxNaPnna-XsecIbxCgfhvzA20BKAooRV3gA7ZBhVWhEMRDtgGQssBGfjtjT2K8BoBKQPWYnQlRZ2VTbdjPXSjMzLHk5i4mshPxOfhEOhK3E7892kTcOH9DgZ_vgh28s8vIA800xdfcRu680c7-oJ4nz9OROE29n52OozWZS9YsLiv01K-0jtEbq1PGb206rs0OQY9jjg05x3vSOdsvwU6HHNyQ8_NIU-J-4ClocyQd7jg5WpPxKXs0aBfp2f2_ZVcf3u8uPhWXXz5-vnh3WRjZqlToaugl7iXWCKYGUkor1UtZghxqFPVeAJVKqVYZJFEZo3tTtU0j-rbXZiC5Zeenunnc7wvF1I02rvPqifwSO5TYYlPlGhl99Q967Zcw5elWqmnKpsq2bBmeKBN8jIGGbg52zKt1CN3qbXfytsvedqu3WbxlL-4rL_t8rz-K32ZmQJyAOK_no_BX6_9UfXkSDdp3-hBs7K6-CsASAFuRF5K_AD34uzw</recordid><startdate>20130401</startdate><enddate>20130401</enddate><creator>Mulisch, Maria</creator><creator>Asp, Torben</creator><creator>Krupinska, Karin</creator><creator>Hollmann, Julien</creator><creator>Holm, Preben Bach</creator><general>Springer-Verlag</general><general>Springer Vienna</general><general>Springer Nature B.V</general><scope>FBQ</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>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88G</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PSYQQ</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20130401</creationdate><title>Tr-cp 14 cysteine protease in white clover (Trifolium repens) is localized to the endoplasmic reticulum and is associated with programmed cell death during development of tracheary elements</title><author>Mulisch, Maria ; Asp, Torben ; Krupinska, Karin ; Hollmann, Julien ; Holm, Preben Bach</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c396t-a5fd31b31710c70e66a66d33403f7127b20e466696c1e25ccadc59882d9dacfe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>apoptosis</topic><topic>Arabidopsis thaliana</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Biology</topic><topic>Cysteine Proteases - genetics</topic><topic>Cysteine Proteases - metabolism</topic><topic>cysteine proteinases</topic><topic>endoplasmic reticulum</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>flowers</topic><topic>Flowers - enzymology</topic><topic>Flowers - metabolism</topic><topic>Life Sciences</topic><topic>pathogens</topic><topic>petioles</topic><topic>Plant Leaves - enzymology</topic><topic>Plant Leaves - metabolism</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Sciences</topic><topic>senescence</topic><topic>Short Communication</topic><topic>tonoplast</topic><topic>tracheary elements</topic><topic>Trifolium - cytology</topic><topic>Trifolium - enzymology</topic><topic>Trifolium repens</topic><topic>vacuoles</topic><topic>Zinnia violacea</topic><topic>Zoology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mulisch, Maria</creatorcontrib><creatorcontrib>Asp, Torben</creatorcontrib><creatorcontrib>Krupinska, Karin</creatorcontrib><creatorcontrib>Hollmann, Julien</creatorcontrib><creatorcontrib>Holm, Preben Bach</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nursing & Allied Health Database</collection><collection>Health & Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Psychology Database (ProQuest)</collection><collection>ProQuest Biological Science Journals</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest One Psychology</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Protoplasma</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mulisch, Maria</au><au>Asp, Torben</au><au>Krupinska, Karin</au><au>Hollmann, Julien</au><au>Holm, Preben Bach</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tr-cp 14 cysteine protease in white clover (Trifolium repens) is localized to the endoplasmic reticulum and is associated with programmed cell death during development of tracheary elements</atitle><jtitle>Protoplasma</jtitle><stitle>Protoplasma</stitle><addtitle>Protoplasma</addtitle><date>2013-04-01</date><risdate>2013</risdate><volume>250</volume><issue>2</issue><spage>623</spage><epage>629</epage><pages>623-629</pages><issn>0033-183X</issn><eissn>1615-6102</eissn><abstract>Cysteine proteases are known to be associated with programmed cell death, developmental senescence and some types of pathogen and stress-induced responses. In the present study, we have characterized the cysteine protease Tr-cp 14 in white clover (Trifolium repens). Tr-cp 14 belongs to the C1A family of cysteine proteases with homology to XCP1 and XCP2 from Arabidopsis thaliana and p48h-17 from Zinnia elegans, which previously have been reported to be associated with tracheary element differentiation. The proform as well as the processed form of the protein was detected in petioles, flowers and leaves, but the processed form was more abundant in leaves and petioles than in flowers. The Tr-cp 14 protein was localized to differentiating tracheary elements within the xylem, indicating that the cysteine protease is involved in protein re-mobilization during tracheary element differentiation. Immunogold studies suggest that the protease prior to the burst of the vacuole was associated to the ER cisternae. After disruption of the tonoplast, it was found in the cytoplasm, and, in later stages, associated with disintegrating material dispersed throughout the cell.</abstract><cop>Vienna</cop><pub>Springer-Verlag</pub><pmid>22707085</pmid><doi>10.1007/s00709-012-0427-1</doi><tpages>7</tpages></addata></record> |
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| subjects | apoptosis Arabidopsis thaliana Biomedical and Life Sciences Cell Biology Cysteine Proteases - genetics Cysteine Proteases - metabolism cysteine proteinases endoplasmic reticulum Endoplasmic Reticulum - metabolism flowers Flowers - enzymology Flowers - metabolism Life Sciences pathogens petioles Plant Leaves - enzymology Plant Leaves - metabolism Plant Proteins - genetics Plant Proteins - metabolism Plant Sciences senescence Short Communication tonoplast tracheary elements Trifolium - cytology Trifolium - enzymology Trifolium repens vacuoles Zinnia violacea Zoology |
| title | Tr-cp 14 cysteine protease in white clover (Trifolium repens) is localized to the endoplasmic reticulum and is associated with programmed cell death during development of tracheary elements |
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