Differential regulation of the durum wheat Pathogenesis-related protein (PR1) by Calmodulin TdCaM1.3 protein
In plants, pathogenesis-related 1 protein (PR1) is considered as important defense protein. The production and accumulation of PR proteins in plants are one of the important responses to several biotic and abiotic stresses. In this regard, PR1 gene was isolated from Triticum turgidum ssp durum and w...
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| Veröffentlicht in: | Molecular biology reports 2021, Vol.48 (1), p.347-362 |
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| creator | Ghorbel, Mouna Zribi, Ikram Missaoui, Khawla Drira-Fakhfekh, Marwa Azzouzi, Basma Brini, Faiçal |
| description | In plants, pathogenesis-related 1 protein (PR1) is considered as important defense protein. The production and accumulation of PR proteins in plants are one of the important responses to several biotic and abiotic stresses. In this regard,
PR1
gene was isolated from
Triticum turgidum
ssp
durum
and was named as
TdPR1.2
. The amino acid sequence of TdPR1.2 protein showed 100%, 97.13%, and 44.41% with known PR1 proteins isolated from
Triticum aestivum
TdPR1-18, PRB1.2 of
Aegilops tauschii
subsp. tauschii and
Arabidopsis thaliana
respectively. qRT-PCR showed that TdPR1.2 was induced specially in leaves of durum wheat treated with Salicylic acid for 48 h. Besides, bioinformatic analysis showed that the durum wheat TdPR1.2 harbors a calmodulin binding domain located in it’s C-terminal part and that this domain is conserved among different PR1 proteins isolated so far. However, no information is available about the regulation of
PR
genes by calmodulin and Ca
2+
complex (CaM/Ca
2+
). Here, we showed that
TdPR1.2
gene exhibits an antibacterial effect as revealed by the in vitro tests against 8 different bacteria and against the fungi
Septoria tritici
. In addition, we demonstrate for the first time that PR1 proteins are able to bind to CaM in a Ca
2+
-dependent manner via a GST-Pull down assay. Finally, in presence of Mn
2+
cations, CaM/Ca
2+
complex stimulated the antimicrobial effect of TdPR1.2. Such effects were not reported so far, and raise a possible role for CaM/Ca
2+
complex in the regulation of plant PRs during cellular response to external signals. |
| doi_str_mv | 10.1007/s11033-020-06053-7 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2470023335</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2470023335</sourcerecordid><originalsourceid>FETCH-LOGICAL-c375t-1cda1f2f66fef2a8fc18fc6cb8290905e7cd61117f8323c768c852b538c26fa53</originalsourceid><addsrcrecordid>eNp9kU1PHDEMhqMKVJYtf6AHFIkLPYTayWQye6y2La0EAlVwjrIZZ3fQfNBkRoh_T-guReLAwbJkP35t-WXsM8IZApivCRGUEiBBQAlaCfOBzVAbJYqFqfbYDBSgKCqNB-wwpTsAKNDoj-xAKYVqYWDG2u9NCBSpHxvX8kjrqXVjM_R8CHzcEK-nOHX8YUNu5Ndu3Axr6ik1SUTKINX8Pg4jNT0_vf6DX_jqkS9d2w311ObaTb10l3imXqBPbD-4NtHRLs_Z7c8fN8tf4uLq_Pfy24XwyuhRoK8dBhnKMlCQrgoec5R-VckFLECT8XWJiCZUSipvyspXWq60qrwsg9Nqzk63unnv34nSaLsmeWpb19MwJSsLAyDzE57Rkzfo3TDFPl9npTbGFKUEyJTcUj4OKUUK9j42nYuPFsE-e2G3Xtjshf3nhTV56HgnPa06qv-PvDw_A2oLpNzq1xRfd78j-wRKXpNp</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2577746200</pqid></control><display><type>article</type><title>Differential regulation of the durum wheat Pathogenesis-related protein (PR1) by Calmodulin TdCaM1.3 protein</title><source>SpringerLink Journals</source><creator>Ghorbel, Mouna ; Zribi, Ikram ; Missaoui, Khawla ; Drira-Fakhfekh, Marwa ; Azzouzi, Basma ; Brini, Faiçal</creator><creatorcontrib>Ghorbel, Mouna ; Zribi, Ikram ; Missaoui, Khawla ; Drira-Fakhfekh, Marwa ; Azzouzi, Basma ; Brini, Faiçal</creatorcontrib><description>In plants, pathogenesis-related 1 protein (PR1) is considered as important defense protein. The production and accumulation of PR proteins in plants are one of the important responses to several biotic and abiotic stresses. In this regard,
PR1
gene was isolated from
Triticum turgidum
ssp
durum
and was named as
TdPR1.2
. The amino acid sequence of TdPR1.2 protein showed 100%, 97.13%, and 44.41% with known PR1 proteins isolated from
Triticum aestivum
TdPR1-18, PRB1.2 of
Aegilops tauschii
subsp. tauschii and
Arabidopsis thaliana
respectively. qRT-PCR showed that TdPR1.2 was induced specially in leaves of durum wheat treated with Salicylic acid for 48 h. Besides, bioinformatic analysis showed that the durum wheat TdPR1.2 harbors a calmodulin binding domain located in it’s C-terminal part and that this domain is conserved among different PR1 proteins isolated so far. However, no information is available about the regulation of
PR
genes by calmodulin and Ca
2+
complex (CaM/Ca
2+
). Here, we showed that
TdPR1.2
gene exhibits an antibacterial effect as revealed by the in vitro tests against 8 different bacteria and against the fungi
Septoria tritici
. In addition, we demonstrate for the first time that PR1 proteins are able to bind to CaM in a Ca
2+
-dependent manner via a GST-Pull down assay. Finally, in presence of Mn
2+
cations, CaM/Ca
2+
complex stimulated the antimicrobial effect of TdPR1.2. Such effects were not reported so far, and raise a possible role for CaM/Ca
2+
complex in the regulation of plant PRs during cellular response to external signals.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-020-06053-7</identifier><identifier>PMID: 33313970</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Amino acid sequence ; Animal Anatomy ; Animal Biochemistry ; Antibacterial activity ; Biomedical and Life Sciences ; Calcium-binding protein ; Calmodulin ; Gene regulation ; Histology ; Life Sciences ; Morphology ; Original Article ; Pathogenesis ; Proteins ; Salicylic acid ; Triticum durum</subject><ispartof>Molecular biology reports, 2021, Vol.48 (1), p.347-362</ispartof><rights>The Author(s), under exclusive licence to Springer Nature B.V. part of Springer Nature 2020</rights><rights>The Author(s), under exclusive licence to Springer Nature B.V. part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-1cda1f2f66fef2a8fc18fc6cb8290905e7cd61117f8323c768c852b538c26fa53</citedby><cites>FETCH-LOGICAL-c375t-1cda1f2f66fef2a8fc18fc6cb8290905e7cd61117f8323c768c852b538c26fa53</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/s11033-020-06053-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11033-020-06053-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33313970$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ghorbel, Mouna</creatorcontrib><creatorcontrib>Zribi, Ikram</creatorcontrib><creatorcontrib>Missaoui, Khawla</creatorcontrib><creatorcontrib>Drira-Fakhfekh, Marwa</creatorcontrib><creatorcontrib>Azzouzi, Basma</creatorcontrib><creatorcontrib>Brini, Faiçal</creatorcontrib><title>Differential regulation of the durum wheat Pathogenesis-related protein (PR1) by Calmodulin TdCaM1.3 protein</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><addtitle>Mol Biol Rep</addtitle><description>In plants, pathogenesis-related 1 protein (PR1) is considered as important defense protein. The production and accumulation of PR proteins in plants are one of the important responses to several biotic and abiotic stresses. In this regard,
PR1
gene was isolated from
Triticum turgidum
ssp
durum
and was named as
TdPR1.2
. The amino acid sequence of TdPR1.2 protein showed 100%, 97.13%, and 44.41% with known PR1 proteins isolated from
Triticum aestivum
TdPR1-18, PRB1.2 of
Aegilops tauschii
subsp. tauschii and
Arabidopsis thaliana
respectively. qRT-PCR showed that TdPR1.2 was induced specially in leaves of durum wheat treated with Salicylic acid for 48 h. Besides, bioinformatic analysis showed that the durum wheat TdPR1.2 harbors a calmodulin binding domain located in it’s C-terminal part and that this domain is conserved among different PR1 proteins isolated so far. However, no information is available about the regulation of
PR
genes by calmodulin and Ca
2+
complex (CaM/Ca
2+
). Here, we showed that
TdPR1.2
gene exhibits an antibacterial effect as revealed by the in vitro tests against 8 different bacteria and against the fungi
Septoria tritici
. In addition, we demonstrate for the first time that PR1 proteins are able to bind to CaM in a Ca
2+
-dependent manner via a GST-Pull down assay. Finally, in presence of Mn
2+
cations, CaM/Ca
2+
complex stimulated the antimicrobial effect of TdPR1.2. Such effects were not reported so far, and raise a possible role for CaM/Ca
2+
complex in the regulation of plant PRs during cellular response to external signals.</description><subject>Amino acid sequence</subject><subject>Animal Anatomy</subject><subject>Animal Biochemistry</subject><subject>Antibacterial activity</subject><subject>Biomedical and Life Sciences</subject><subject>Calcium-binding protein</subject><subject>Calmodulin</subject><subject>Gene regulation</subject><subject>Histology</subject><subject>Life Sciences</subject><subject>Morphology</subject><subject>Original Article</subject><subject>Pathogenesis</subject><subject>Proteins</subject><subject>Salicylic acid</subject><subject>Triticum durum</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kU1PHDEMhqMKVJYtf6AHFIkLPYTayWQye6y2La0EAlVwjrIZZ3fQfNBkRoh_T-guReLAwbJkP35t-WXsM8IZApivCRGUEiBBQAlaCfOBzVAbJYqFqfbYDBSgKCqNB-wwpTsAKNDoj-xAKYVqYWDG2u9NCBSpHxvX8kjrqXVjM_R8CHzcEK-nOHX8YUNu5Ndu3Axr6ik1SUTKINX8Pg4jNT0_vf6DX_jqkS9d2w311ObaTb10l3imXqBPbD-4NtHRLs_Z7c8fN8tf4uLq_Pfy24XwyuhRoK8dBhnKMlCQrgoec5R-VckFLECT8XWJiCZUSipvyspXWq60qrwsg9Nqzk63unnv34nSaLsmeWpb19MwJSsLAyDzE57Rkzfo3TDFPl9npTbGFKUEyJTcUj4OKUUK9j42nYuPFsE-e2G3Xtjshf3nhTV56HgnPa06qv-PvDw_A2oLpNzq1xRfd78j-wRKXpNp</recordid><startdate>2021</startdate><enddate>2021</enddate><creator>Ghorbel, Mouna</creator><creator>Zribi, Ikram</creator><creator>Missaoui, Khawla</creator><creator>Drira-Fakhfekh, Marwa</creator><creator>Azzouzi, Basma</creator><creator>Brini, Faiçal</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</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>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>2021</creationdate><title>Differential regulation of the durum wheat Pathogenesis-related protein (PR1) by Calmodulin TdCaM1.3 protein</title><author>Ghorbel, Mouna ; Zribi, Ikram ; Missaoui, Khawla ; Drira-Fakhfekh, Marwa ; Azzouzi, Basma ; Brini, Faiçal</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-1cda1f2f66fef2a8fc18fc6cb8290905e7cd61117f8323c768c852b538c26fa53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Amino acid sequence</topic><topic>Animal Anatomy</topic><topic>Animal Biochemistry</topic><topic>Antibacterial activity</topic><topic>Biomedical and Life Sciences</topic><topic>Calcium-binding protein</topic><topic>Calmodulin</topic><topic>Gene regulation</topic><topic>Histology</topic><topic>Life Sciences</topic><topic>Morphology</topic><topic>Original Article</topic><topic>Pathogenesis</topic><topic>Proteins</topic><topic>Salicylic acid</topic><topic>Triticum durum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ghorbel, Mouna</creatorcontrib><creatorcontrib>Zribi, Ikram</creatorcontrib><creatorcontrib>Missaoui, Khawla</creatorcontrib><creatorcontrib>Drira-Fakhfekh, Marwa</creatorcontrib><creatorcontrib>Azzouzi, Basma</creatorcontrib><creatorcontrib>Brini, Faiçal</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</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>Engineering Research Database</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 & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</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 Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular biology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ghorbel, Mouna</au><au>Zribi, Ikram</au><au>Missaoui, Khawla</au><au>Drira-Fakhfekh, Marwa</au><au>Azzouzi, Basma</au><au>Brini, Faiçal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential regulation of the durum wheat Pathogenesis-related protein (PR1) by Calmodulin TdCaM1.3 protein</atitle><jtitle>Molecular biology reports</jtitle><stitle>Mol Biol Rep</stitle><addtitle>Mol Biol Rep</addtitle><date>2021</date><risdate>2021</risdate><volume>48</volume><issue>1</issue><spage>347</spage><epage>362</epage><pages>347-362</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>In plants, pathogenesis-related 1 protein (PR1) is considered as important defense protein. The production and accumulation of PR proteins in plants are one of the important responses to several biotic and abiotic stresses. In this regard,
PR1
gene was isolated from
Triticum turgidum
ssp
durum
and was named as
TdPR1.2
. The amino acid sequence of TdPR1.2 protein showed 100%, 97.13%, and 44.41% with known PR1 proteins isolated from
Triticum aestivum
TdPR1-18, PRB1.2 of
Aegilops tauschii
subsp. tauschii and
Arabidopsis thaliana
respectively. qRT-PCR showed that TdPR1.2 was induced specially in leaves of durum wheat treated with Salicylic acid for 48 h. Besides, bioinformatic analysis showed that the durum wheat TdPR1.2 harbors a calmodulin binding domain located in it’s C-terminal part and that this domain is conserved among different PR1 proteins isolated so far. However, no information is available about the regulation of
PR
genes by calmodulin and Ca
2+
complex (CaM/Ca
2+
). Here, we showed that
TdPR1.2
gene exhibits an antibacterial effect as revealed by the in vitro tests against 8 different bacteria and against the fungi
Septoria tritici
. In addition, we demonstrate for the first time that PR1 proteins are able to bind to CaM in a Ca
2+
-dependent manner via a GST-Pull down assay. Finally, in presence of Mn
2+
cations, CaM/Ca
2+
complex stimulated the antimicrobial effect of TdPR1.2. Such effects were not reported so far, and raise a possible role for CaM/Ca
2+
complex in the regulation of plant PRs during cellular response to external signals.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>33313970</pmid><doi>10.1007/s11033-020-06053-7</doi><tpages>16</tpages></addata></record> |
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| subjects | Amino acid sequence Animal Anatomy Animal Biochemistry Antibacterial activity Biomedical and Life Sciences Calcium-binding protein Calmodulin Gene regulation Histology Life Sciences Morphology Original Article Pathogenesis Proteins Salicylic acid Triticum durum |
| title | Differential regulation of the durum wheat Pathogenesis-related protein (PR1) by Calmodulin TdCaM1.3 protein |
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