Lipid binding activities of flax rust AvrM and AvrL567 effectors.
Identifieur interne : 000145 ( Main/Exploration ); précédent : 000144; suivant : 000146Lipid binding activities of flax rust AvrM and AvrL567 effectors.
Auteurs : Pamela H P. Gan [Australie] ; Maryam Rafiqi ; Jeffrey G. Ellis ; David A. Jones ; Adrienne R. Hardham ; Peter N. DoddsSource :
- Plant signaling & behavior [ 1559-2324 ] ; 2010.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Mutation.
- microbiologie : Lin, Maladies des plantes.
- métabolisme : Protéines fongiques.
- physiologie : Basidiomycota.
- Liaison aux protéines, Métabolisme lipidique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Fungal Proteins.
- genetics : Mutation.
- microbiology : Flax, Plant Diseases.
- physiology : Basidiomycota.
- Lipid Metabolism, Protein Binding.
Abstract
Effectors are pathogen-encoded proteins that are thought to facilitate infection by manipulation of host cells. Evidence showing that the effectors of some eukaryotic plant pathogens are able to interact directly with cytoplasmic host proteins indicates that translocation of these proteins into host cells is an important part of infection. Recently, we showed that the flax rust effectors AvrM and AvrL567 are able to internalize into plant cells in the absence of the pathogen. Further, N-terminal sequences that were sufficient for uptake were identified for both these proteins. In light of the possibility that the internalization of fungal and oomycete effectors may require binding to specific phospholipids, the lipid binding activities of AvrM and AvrL567 mutants with different abilities to enter cells were tested. While AvrL567 was not found to bind to phospholipids, AvrM bound strongly to phosphatidyl inositol, phosphatidyl inositol monophosphates and phosphatidyl serine. However, a fragment of AvrM sufficient to direct uptake of a fusion protein into plant cells did not bind to these phospholipids. Thus, our results do not support the role of specific binding of AvrM and AvrL567 to phospholipids for uptake into the plant cytoplasm.
DOI: 10.4161/psb.5.10.13013
PubMed: 20855950
PubMed Central: PMC3115366
Affiliations:
Links toward previous steps (curation, corpus...)
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Gan</name><affiliation wicri:level="1"><nlm:affiliation>Plant Science Division, Research School of Biology, College of Medicine, Biology and Environment, The Australian National University, Canberra, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Plant Science Division, Research School of Biology, College of Medicine, Biology and Environment, The Australian National University, Canberra</wicri:regionArea><wicri:noRegion>Canberra</wicri:noRegion></affiliation></author><author><name sortKey="Rafiqi, Maryam" sort="Rafiqi, Maryam" uniqKey="Rafiqi M" first="Maryam" last="Rafiqi">Maryam Rafiqi</name></author><author><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name></author><author><name sortKey="Jones, David A" sort="Jones, David A" uniqKey="Jones D" first="David A" last="Jones">David A. Jones</name></author><author><name sortKey="Hardham, Adrienne R" sort="Hardham, Adrienne R" uniqKey="Hardham A" first="Adrienne R" last="Hardham">Adrienne R. Hardham</name></author><author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. 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Jones</name></author><author><name sortKey="Hardham, Adrienne R" sort="Hardham, Adrienne R" uniqKey="Hardham A" first="Adrienne R" last="Hardham">Adrienne R. Hardham</name></author><author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name></author></analytic><series><title level="j">Plant signaling & behavior</title><idno type="eISSN">1559-2324</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (physiology)</term><term>Flax (microbiology)</term><term>Fungal Proteins (metabolism)</term><term>Lipid Metabolism (MeSH)</term><term>Mutation (genetics)</term><term>Plant Diseases (microbiology)</term><term>Protein Binding (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (physiologie)</term><term>Liaison aux protéines (MeSH)</term><term>Lin (microbiologie)</term><term>Maladies des plantes (microbiologie)</term><term>Mutation (génétique)</term><term>Métabolisme lipidique (MeSH)</term><term>Protéines fongiques (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Lin</term><term>Maladies des plantes</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Flax</term><term>Plant Diseases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Lipid Metabolism</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Liaison aux protéines</term><term>Métabolisme lipidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Effectors are pathogen-encoded proteins that are thought to facilitate infection by manipulation of host cells. Evidence showing that the effectors of some eukaryotic plant pathogens are able to interact directly with cytoplasmic host proteins indicates that translocation of these proteins into host cells is an important part of infection. Recently, we showed that the flax rust effectors AvrM and AvrL567 are able to internalize into plant cells in the absence of the pathogen. Further, N-terminal sequences that were sufficient for uptake were identified for both these proteins. In light of the possibility that the internalization of fungal and oomycete effectors may require binding to specific phospholipids, the lipid binding activities of AvrM and AvrL567 mutants with different abilities to enter cells were tested. While AvrL567 was not found to bind to phospholipids, AvrM bound strongly to phosphatidyl inositol, phosphatidyl inositol monophosphates and phosphatidyl serine. However, a fragment of AvrM sufficient to direct uptake of a fusion protein into plant cells did not bind to these phospholipids. Thus, our results do not support the role of specific binding of AvrM and AvrL567 to phospholipids for uptake into the plant cytoplasm.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20855950</PMID><DateCompleted><Year>2011</Year><Month>08</Month><Day>26</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1559-2324</ISSN><JournalIssue CitedMedium="Internet"><Volume>5</Volume><Issue>10</Issue><PubDate><Year>2010</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Plant signaling & behavior</Title><ISOAbbreviation>Plant Signal Behav</ISOAbbreviation></Journal><ArticleTitle>Lipid binding activities of flax rust AvrM and AvrL567 effectors.</ArticleTitle><Pagination><MedlinePgn>1272-5</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.4161/psb.5.10.13013</ELocationID><Abstract><AbstractText>Effectors are pathogen-encoded proteins that are thought to facilitate infection by manipulation of host cells. Evidence showing that the effectors of some eukaryotic plant pathogens are able to interact directly with cytoplasmic host proteins indicates that translocation of these proteins into host cells is an important part of infection. Recently, we showed that the flax rust effectors AvrM and AvrL567 are able to internalize into plant cells in the absence of the pathogen. Further, N-terminal sequences that were sufficient for uptake were identified for both these proteins. In light of the possibility that the internalization of fungal and oomycete effectors may require binding to specific phospholipids, the lipid binding activities of AvrM and AvrL567 mutants with different abilities to enter cells were tested. While AvrL567 was not found to bind to phospholipids, AvrM bound strongly to phosphatidyl inositol, phosphatidyl inositol monophosphates and phosphatidyl serine. However, a fragment of AvrM sufficient to direct uptake of a fusion protein into plant cells did not bind to these phospholipids. Thus, our results do not support the role of specific binding of AvrM and AvrL567 to phospholipids for uptake into the plant cytoplasm.</AbstractText><CopyrightInformation>© 2010 Landes Bioscience</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gan</LastName><ForeName>Pamela H P</ForeName><Initials>PH</Initials><AffiliationInfo><Affiliation>Plant Science Division, Research School of Biology, College of Medicine, Biology and Environment, The Australian National University, Canberra, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rafiqi</LastName><ForeName>Maryam</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ellis</LastName><ForeName>Jeffrey G</ForeName><Initials>JG</Initials></Author><Author ValidYN="Y"><LastName>Jones</LastName><ForeName>David A</ForeName><Initials>DA</Initials></Author><Author ValidYN="Y"><LastName>Hardham</LastName><ForeName>Adrienne R</ForeName><Initials>AR</Initials></Author><Author ValidYN="Y"><LastName>Dodds</LastName><ForeName>Peter N</ForeName><Initials>PN</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>10</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Signal Behav</MedlineTA><NlmUniqueID>101291431</NlmUniqueID><ISSNLinking>1559-2316</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019597" MajorTopicYN="N">Flax</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050356" MajorTopicYN="Y">Lipid Metabolism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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IdType="pubmed">20525849</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country></list><tree><noCountry><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name><name sortKey="Hardham, Adrienne R" sort="Hardham, Adrienne R" uniqKey="Hardham A" first="Adrienne R" last="Hardham">Adrienne R. Hardham</name><name sortKey="Jones, David A" sort="Jones, David A" uniqKey="Jones D" first="David A" last="Jones">David A. Jones</name><name sortKey="Rafiqi, Maryam" sort="Rafiqi, Maryam" uniqKey="Rafiqi M" first="Maryam" last="Rafiqi">Maryam Rafiqi</name></noCountry><country name="Australie"><noRegion><name sortKey="Gan, Pamela H P" sort="Gan, Pamela H P" uniqKey="Gan P" first="Pamela H P" last="Gan">Pamela H P. Gan</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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