Temperature-induced lipocalin (TIL) is translocated under salt stress and protects chloroplasts from ion toxicity.
Identifieur interne : 002469 ( Main/Corpus ); précédent : 002468; suivant : 002470Temperature-induced lipocalin (TIL) is translocated under salt stress and protects chloroplasts from ion toxicity.
Auteurs : Atef Abo-Ogiala ; Caroline Carsjens ; Heike Diekmann ; Payam Fayyaz ; Cornelia Herrfurth ; Ivo Feussner ; Andrea PolleSource :
- Journal of plant physiology [ 1618-1328 ] ; 2014.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lipocalins.
- chemical , pharmacology : Sodium Chloride.
- chemical , toxicity : Iron.
- drug effects : Chloroplasts.
- metabolism : Chloroplasts.
- Temperature.
Abstract
Temperature-induced lipocalins (TIL) have been invoked in the defense from heat, cold and oxidative stress. Here we document a function of TIL for basal protection from salinity stress. Heterologous expression of TIL from the salt resistant poplar Populus euphratica did not rescue growth but prevented chlorophyll b destruction in salt-exposed Arabidopsis thaliana. The protein was localized to the plasma membrane but was re-translocated to the symplast under salt stress. The A. thaliana knock out and knock down lines Attil1-1 and Attil1-2 showed stronger stress symptoms and stronger chlorophyll b degradation than the wildtype (WT) under excess salinity. They accumulated more chloride and sodium in chloroplasts than the WT. Chloroplast chloride accumulation was found even in the absence of salt stress. Since lipocalins are known to bind regulatory fatty acids of channel proteins as well as iron, we suggest that the salt-induced trafficking of TIL may be required for protection of chloroplasts by affecting ion homeostasis.
DOI: 10.1016/j.jplph.2013.08.003
PubMed: 24028869
Links to Exploration step
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Electronic address: apolle@gwdg.de.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of plant physiology</title><idno type="eISSN">1618-1328</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chloroplasts (drug effects)</term><term>Chloroplasts (metabolism)</term><term>Iron (toxicity)</term><term>Lipocalins (metabolism)</term><term>Sodium Chloride (pharmacology)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lipocalins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sodium Chloride</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Iron</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Chloroplasts</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Chloroplasts</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Temperature-induced lipocalins (TIL) have been invoked in the defense from heat, cold and oxidative stress. Here we document a function of TIL for basal protection from salinity stress. Heterologous expression of TIL from the salt resistant poplar Populus euphratica did not rescue growth but prevented chlorophyll b destruction in salt-exposed Arabidopsis thaliana. The protein was localized to the plasma membrane but was re-translocated to the symplast under salt stress. The A. thaliana knock out and knock down lines Attil1-1 and Attil1-2 showed stronger stress symptoms and stronger chlorophyll b degradation than the wildtype (WT) under excess salinity. They accumulated more chloride and sodium in chloroplasts than the WT. Chloroplast chloride accumulation was found even in the absence of salt stress. Since lipocalins are known to bind regulatory fatty acids of channel proteins as well as iron, we suggest that the salt-induced trafficking of TIL may be required for protection of chloroplasts by affecting ion homeostasis. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24028869</PMID><DateCompleted><Year>2014</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1618-1328</ISSN><JournalIssue CitedMedium="Internet"><Volume>171</Volume><Issue>3-4</Issue><PubDate><Year>2014</Year><Month>Feb</Month><Day>15</Day></PubDate></JournalIssue><Title>Journal of plant physiology</Title><ISOAbbreviation>J Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Temperature-induced lipocalin (TIL) is translocated under salt stress and protects chloroplasts from ion toxicity.</ArticleTitle><Pagination><MedlinePgn>250-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jplph.2013.08.003</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0176-1617(13)00319-2</ELocationID><Abstract><AbstractText>Temperature-induced lipocalins (TIL) have been invoked in the defense from heat, cold and oxidative stress. Here we document a function of TIL for basal protection from salinity stress. Heterologous expression of TIL from the salt resistant poplar Populus euphratica did not rescue growth but prevented chlorophyll b destruction in salt-exposed Arabidopsis thaliana. The protein was localized to the plasma membrane but was re-translocated to the symplast under salt stress. The A. thaliana knock out and knock down lines Attil1-1 and Attil1-2 showed stronger stress symptoms and stronger chlorophyll b degradation than the wildtype (WT) under excess salinity. They accumulated more chloride and sodium in chloroplasts than the WT. Chloroplast chloride accumulation was found even in the absence of salt stress. Since lipocalins are known to bind regulatory fatty acids of channel proteins as well as iron, we suggest that the salt-induced trafficking of TIL may be required for protection of chloroplasts by affecting ion homeostasis. </AbstractText><CopyrightInformation>Copyright © 2013 Elsevier GmbH. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Abo-Ogiala</LastName><ForeName>Atef</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Forest Botany and Tree Physiology, Büsgen-Institute, Georg-August University Göttingen, Büsgenweg 2, 37077 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carsjens</LastName><ForeName>Caroline</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Forest Botany and Tree Physiology, Büsgen-Institute, Georg-August University Göttingen, Büsgenweg 2, 37077 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Diekmann</LastName><ForeName>Heike</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Forest Botany and Tree Physiology, Büsgen-Institute, Georg-August University Göttingen, Büsgenweg 2, 37077 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fayyaz</LastName><ForeName>Payam</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Forest Botany and Tree Physiology, Büsgen-Institute, Georg-August University Göttingen, Büsgenweg 2, 37077 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrfurth</LastName><ForeName>Cornelia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Science, Justus-von-Liebig-Weg 11, Georg-August University Göttingen, 37077 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Feussner</LastName><ForeName>Ivo</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Science, Justus-von-Liebig-Weg 11, Georg-August University Göttingen, 37077 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Polle</LastName><ForeName>Andrea</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Forest Botany and Tree Physiology, Büsgen-Institute, Georg-August University Göttingen, Büsgenweg 2, 37077 Göttingen, Germany. Electronic address: apolle@gwdg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>09</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>J Plant Physiol</MedlineTA><NlmUniqueID>9882059</NlmUniqueID><ISSNLinking>0176-1617</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054834">Lipocalins</NameOfSubstance></Chemical><Chemical><RegistryNumber>451W47IQ8X</RegistryNumber><NameOfSubstance UI="D012965">Sodium Chloride</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002736" MajorTopicYN="N">Chloroplasts</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054834" MajorTopicYN="N">Lipocalins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012965" MajorTopicYN="N">Sodium Chloride</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="Y">Temperature</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Apolipoprotein</Keyword><Keyword MajorTopicYN="N">Arabidopsis</Keyword><Keyword MajorTopicYN="N">Populus</Keyword><Keyword MajorTopicYN="N">Salt resistance</Keyword><Keyword MajorTopicYN="N">Stress</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>06</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>08</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>08</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>10</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24028869</ArticleId><ArticleId IdType="pii">S0176-1617(13)00319-2</ArticleId><ArticleId IdType="doi">10.1016/j.jplph.2013.08.003</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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