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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Protoplasma 2013-04, Vol.250 (2), p.623-629
Hauptverfasser: Mulisch, Maria, Asp, Torben, Krupinska, Karin, Hollmann, Julien, Holm, Preben Bach
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 629
container_issue 2
container_start_page 623
container_title Protoplasma
container_volume 250
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
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1319185466</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1319185466</sourcerecordid><originalsourceid>FETCH-LOGICAL-c396t-a5fd31b31710c70e66a66d33403f7127b20e466696c1e25ccadc59882d9dacfe3</originalsourceid><addsrcrecordid>eNp9kU1v1DAQhi0EosvCD-AClriUQ2DGTpzkiCq-pEoc2ErcIq8z2XXlxMF2WpX_xn_D0RaEOHCxNaPnna-XsecIbxCgfhvzA20BKAooRV3gA7ZBhVWhEMRDtgGQssBGfjtjT2K8BoBKQPWYnQlRZ2VTbdjPXSjMzLHk5i4mshPxOfhEOhK3E7892kTcOH9DgZ_vgh28s8vIA800xdfcRu680c7-oJ4nz9OROE29n52OozWZS9YsLiv01K-0jtEbq1PGb206rs0OQY9jjg05x3vSOdsvwU6HHNyQ8_NIU-J-4ClocyQd7jg5WpPxKXs0aBfp2f2_ZVcf3u8uPhWXXz5-vnh3WRjZqlToaugl7iXWCKYGUkor1UtZghxqFPVeAJVKqVYZJFEZo3tTtU0j-rbXZiC5Zeenunnc7wvF1I02rvPqifwSO5TYYlPlGhl99Q967Zcw5elWqmnKpsq2bBmeKBN8jIGGbg52zKt1CN3qbXfytsvedqu3WbxlL-4rL_t8rz-K32ZmQJyAOK_no_BX6_9UfXkSDdp3-hBs7K6-CsASAFuRF5K_AD34uzw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1318848500</pqid></control><display><type>article</type><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><source>MEDLINE</source><source>SpringerNature Journals</source><creator>Mulisch, Maria ; Asp, Torben ; Krupinska, Karin ; Hollmann, Julien ; Holm, Preben Bach</creator><creatorcontrib>Mulisch, Maria ; Asp, Torben ; Krupinska, Karin ; Hollmann, Julien ; Holm, Preben Bach</creatorcontrib><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><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 &amp; Allied Health Database</collection><collection>Health &amp; Medical Collection</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 Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Nursing &amp; Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Psychology Database</collection><collection>Biological Science Database</collection><collection>Nursing &amp; 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>
fulltext fulltext
identifier ISSN: 0033-183X
ispartof Protoplasma, 2013-04, Vol.250 (2), p.623-629
issn 0033-183X
1615-6102
language eng
recordid cdi_proquest_miscellaneous_1319185466
source MEDLINE; SpringerNature Journals
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-05T19%3A15%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Tr-cp%2014%20cysteine%20protease%20in%20white%20clover%20(Trifolium%20repens)%20is%20localized%20to%20the%20endoplasmic%20reticulum%20and%20is%20associated%20with%20programmed%20cell%20death%20during%20development%20of%20tracheary%20elements&rft.jtitle=Protoplasma&rft.au=Mulisch,%20Maria&rft.date=2013-04-01&rft.volume=250&rft.issue=2&rft.spage=623&rft.epage=629&rft.pages=623-629&rft.issn=0033-183X&rft.eissn=1615-6102&rft_id=info:doi/10.1007/s00709-012-0427-1&rft_dat=%3Cproquest_cross%3E1319185466%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1318848500&rft_id=info:pmid/22707085&rfr_iscdi=true