Elicitin-membrane interaction is driven by a positive charge on the protein surface: role of Lys13 residue in lipids loading and resistance induction.
Identifieur interne : 001754 ( Main/Exploration ); précédent : 001753; suivant : 001755Elicitin-membrane interaction is driven by a positive charge on the protein surface: role of Lys13 residue in lipids loading and resistance induction.
Auteurs : Veronika Plešková [République tchèque] ; Tomáš Kašparovsk ; Michal Obo Il ; Nikola Ptá Ková ; Radka Chaloupková ; Dokládal Ladislav ; Ji Damborsk ; Jan LochmanSource :
- Plant physiology and biochemistry : PPB [ 1873-2690 ] ; 2011.
Descripteurs français
- KwdFr :
- Acides gras (métabolisme), Expression des gènes (MeSH), Gènes de plante (MeSH), Immunité des plantes (physiologie), Interactions hôte-pathogène (physiologie), Liposomes (métabolisme), Lysine (génétique), Lysine (métabolisme), Maladies des plantes (génétique), Maladies des plantes (microbiologie), Micelles (MeSH), Mutation (MeSH), Métabolisme lipidique (physiologie), Nécrose (MeSH), Oomycetes (pathogénicité), Oomycetes (physiologie), Phytostérols (métabolisme), Protéines d'algue (composition chimique), Protéines d'algue (génétique), Protéines d'algue (métabolisme), Protéines fongiques (MeSH), Transport biologique (MeSH), Valine (métabolisme), Électricité (MeSH).
- MESH :
- composition chimique : Protéines d'algue.
- génétique : Lysine, Maladies des plantes, Protéines d'algue.
- microbiologie : Maladies des plantes.
- métabolisme : Acides gras, Liposomes, Lysine, Phytostérols, Protéines d'algue, Valine.
- pathogénicité : Oomycetes.
- physiologie : Immunité des plantes, Interactions hôte-pathogène, Métabolisme lipidique, Oomycetes.
- Expression des gènes, Gènes de plante, Micelles, Mutation, Nécrose, Protéines fongiques, Transport biologique, Électricité.
English descriptors
- KwdEn :
- Algal Proteins (chemistry), Algal Proteins (genetics), Algal Proteins (metabolism), Biological Transport (MeSH), Electricity (MeSH), Fatty Acids (metabolism), Fungal Proteins (MeSH), Gene Expression (MeSH), Genes, Plant (MeSH), Host-Pathogen Interactions (physiology), Lipid Metabolism (physiology), Liposomes (metabolism), Lysine (genetics), Lysine (metabolism), Micelles (MeSH), Mutation (MeSH), Necrosis (MeSH), Oomycetes (pathogenicity), Oomycetes (physiology), Phytosterols (metabolism), Plant Diseases (genetics), Plant Diseases (microbiology), Plant Immunity (physiology), Valine (metabolism).
- MESH :
- chemical , chemistry : Algal Proteins.
- chemical , genetics : Algal Proteins, Lysine.
- chemical , metabolism : Algal Proteins, Fatty Acids, Liposomes, Lysine, Phytosterols, Valine.
- genetics : Plant Diseases.
- microbiology : Plant Diseases.
- pathogenicity : Oomycetes.
- physiology : Host-Pathogen Interactions, Lipid Metabolism, Oomycetes, Plant Immunity.
- Biological Transport, Electricity, Fungal Proteins, Gene Expression, Genes, Plant, Micelles, Mutation, Necrosis.
Abstract
Elicitins are family of small proteins secreted by species of the pathogenic fungus Phytophthora inducing a defence reaction in plants. They contain a hydrophobic cavity capable of binding sterols and fatty acids, and on the basis of their pI they are classified as either α-elicitins or more necrotising β-elicitins. The residue Lys13 was previously identified as a key determinant of the necrotising activity of basic elicitins. In the present study we describe changes in the ability of cryptogein, a β-elicitin inducing a hypersensitive response in tobacco, to transfer sterols and fatty acids between micelles and liposomes upon Lys13Val mutation. We propose that the change in activity is influenced by the elimination of positive charge on the surface of cryptogein, which is significant for correct positioning of the protein during lipid loading, without adversely affecting the binding of sterol to the cavity of the protein. Compared to wild type cryptogein, mutation Lys13Val resulted in lowered expression of defence-related genes and compromised resistance to Phytophthora parasitica. Furthermore, resistance induced by Lys13Val mutant was similar to that induced by acidic elicitin capsicein containing at amino position 13 valine Determined results sustained a crucial role of positive lysine residues on the surface of basic elicitins and suggested their significant role in correct protein-membrane interaction and thus on their biological activity.
DOI: 10.1016/j.plaphy.2011.01.008
PubMed: 21296584
Affiliations:
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(métabolisme)</term><term>Maladies des plantes (génétique)</term><term>Maladies des plantes (microbiologie)</term><term>Micelles (MeSH)</term><term>Mutation (MeSH)</term><term>Métabolisme lipidique (physiologie)</term><term>Nécrose (MeSH)</term><term>Oomycetes (pathogénicité)</term><term>Oomycetes (physiologie)</term><term>Phytostérols (métabolisme)</term><term>Protéines d'algue (composition chimique)</term><term>Protéines d'algue (génétique)</term><term>Protéines d'algue (métabolisme)</term><term>Protéines fongiques (MeSH)</term><term>Transport biologique (MeSH)</term><term>Valine (métabolisme)</term><term>Électricité (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Algal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Algal Proteins</term><term>Lysine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Algal 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biologique</term><term>Électricité</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Elicitins are family of small proteins secreted by species of the pathogenic fungus Phytophthora inducing a defence reaction in plants. They contain a hydrophobic cavity capable of binding sterols and fatty acids, and on the basis of their pI they are classified as either α-elicitins or more necrotising β-elicitins. The residue Lys13 was previously identified as a key determinant of the necrotising activity of basic elicitins. In the present study we describe changes in the ability of cryptogein, a β-elicitin inducing a hypersensitive response in tobacco, to transfer sterols and fatty acids between micelles and liposomes upon Lys13Val mutation. We propose that the change in activity is influenced by the elimination of positive charge on the surface of cryptogein, which is significant for correct positioning of the protein during lipid loading, without adversely affecting the binding of sterol to the cavity of the protein. Compared to wild type cryptogein, mutation Lys13Val resulted in lowered expression of defence-related genes and compromised resistance to Phytophthora parasitica. Furthermore, resistance induced by Lys13Val mutant was similar to that induced by acidic elicitin capsicein containing at amino position 13 valine Determined results sustained a crucial role of positive lysine residues on the surface of basic elicitins and suggested their significant role in correct protein-membrane interaction and thus on their biological activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21296584</PMID><DateCompleted><Year>2011</Year><Month>10</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2690</ISSN><JournalIssue CitedMedium="Internet"><Volume>49</Volume><Issue>3</Issue><PubDate><Year>2011</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Plant physiology and biochemistry : PPB</Title><ISOAbbreviation>Plant Physiol Biochem</ISOAbbreviation></Journal><ArticleTitle>Elicitin-membrane interaction is driven by a positive charge on the protein surface: role of Lys13 residue in lipids loading and resistance induction.</ArticleTitle><Pagination><MedlinePgn>321-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.plaphy.2011.01.008</ELocationID><Abstract><AbstractText>Elicitins are family of small proteins secreted by species of the pathogenic fungus Phytophthora inducing a defence reaction in plants. They contain a hydrophobic cavity capable of binding sterols and fatty acids, and on the basis of their pI they are classified as either α-elicitins or more necrotising β-elicitins. The residue Lys13 was previously identified as a key determinant of the necrotising activity of basic elicitins. In the present study we describe changes in the ability of cryptogein, a β-elicitin inducing a hypersensitive response in tobacco, to transfer sterols and fatty acids between micelles and liposomes upon Lys13Val mutation. We propose that the change in activity is influenced by the elimination of positive charge on the surface of cryptogein, which is significant for correct positioning of the protein during lipid loading, without adversely affecting the binding of sterol to the cavity of the protein. Compared to wild type cryptogein, mutation Lys13Val resulted in lowered expression of defence-related genes and compromised resistance to Phytophthora parasitica. Furthermore, resistance induced by Lys13Val mutant was similar to that induced by acidic elicitin capsicein containing at amino position 13 valine Determined results sustained a crucial role of positive lysine residues on the surface of basic elicitins and suggested their significant role in correct protein-membrane interaction and thus on their biological activity.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier Masson SAS. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Plešková</LastName><ForeName>Veronika</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and National Center for Biomolecular Research, Faculty of Science, Masaryk University, Kotlářská 2, Brno, Czech Republic.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kašparovský</LastName><ForeName>Tomáš</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Obořil</LastName><ForeName>Michal</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ptáčková</LastName><ForeName>Nikola</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Chaloupková</LastName><ForeName>Radka</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Ladislav</LastName><ForeName>Dokládal</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Damborský</LastName><ForeName>Jiří</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Lochman</LastName><ForeName>Jan</ForeName><Initials>J</Initials></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>2011</Year><Month>01</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Plant Physiol Biochem</MedlineTA><NlmUniqueID>9882449</NlmUniqueID><ISSNLinking>0981-9428</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005227">Fatty Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008081">Liposomes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008823">Micelles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010840">Phytosterols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C061032">cryptogein protein, Phytophthora cryptogea</NameOfSubstance></Chemical><Chemical><RegistryNumber>HG18B9YRS7</RegistryNumber><NameOfSubstance UI="D014633">Valine</NameOfSubstance></Chemical><Chemical><RegistryNumber>K3Z4F929H6</RegistryNumber><NameOfSubstance UI="D008239">Lysine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="N">Algal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004560" MajorTopicYN="N">Electricity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005227" MajorTopicYN="N">Fatty Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017343" MajorTopicYN="N">Genes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="N">Host-Pathogen Interactions</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050356" MajorTopicYN="N">Lipid Metabolism</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008081" MajorTopicYN="N">Liposomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008239" MajorTopicYN="N">Lysine</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008823" MajorTopicYN="N">Micelles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009336" 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UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>10</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2010</Year><Month>12</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>01</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>2</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>2</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>10</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21296584</ArticleId><ArticleId IdType="pii">S0981-9428(11)00009-X</ArticleId><ArticleId IdType="doi">10.1016/j.plaphy.2011.01.008</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République tchèque</li></country><region><li>Moravie</li></region><settlement><li>Brno</li></settlement></list><tree><noCountry><name sortKey="Chaloupkova, Radka" sort="Chaloupkova, Radka" uniqKey="Chaloupkova R" first="Radka" last="Chaloupková">Radka Chaloupková</name><name sortKey="Damborsk, Ji" sort="Damborsk, Ji" uniqKey="Damborsk J" first="Ji" last="Damborsk">Ji Damborsk</name><name sortKey="Kasparovsk, Tomas" sort="Kasparovsk, Tomas" uniqKey="Kasparovsk T" first="Tomáš" last="Kašparovsk">Tomáš Kašparovsk</name><name sortKey="Ladislav, Dokladal" sort="Ladislav, Dokladal" uniqKey="Ladislav D" first="Dokládal" last="Ladislav">Dokládal Ladislav</name><name sortKey="Lochman, Jan" sort="Lochman, Jan" uniqKey="Lochman J" first="Jan" last="Lochman">Jan Lochman</name><name sortKey="Obo Il, Michal" sort="Obo Il, Michal" uniqKey="Obo Il M" first="Michal" last="Obo Il">Michal Obo Il</name><name sortKey="Pta Kova, Nikola" sort="Pta Kova, Nikola" uniqKey="Pta Kova N" first="Nikola" last="Ptá Ková">Nikola Ptá Ková</name></noCountry><country name="République tchèque"><region name="Moravie"><name sortKey="Pleskova, Veronika" sort="Pleskova, Veronika" uniqKey="Pleskova V" first="Veronika" last="Plešková">Veronika Plešková</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhytophthoraV1
| This area was generated with Dilib version V0.6.38. |  |