The RXLR motif of oomycete effectors is not a sufficient element for binding to phosphatidylinositol monophosphates.
Identifieur interne : 000203 ( Main/Exploration ); précédent : 000202; suivant : 000204The RXLR motif of oomycete effectors is not a sufficient element for binding to phosphatidylinositol monophosphates.
Auteurs : Takashi Yaeno [Japon] ; Ken ShirasuSource :
- Plant signaling & behavior [ 1559-2324 ] ; 2013.
Descripteurs français
- KwdFr :
- Arabidopsis (microbiologie), Facteurs de virulence (métabolisme), Immunité des plantes (MeSH), Lysine (métabolisme), Maladies des plantes (microbiologie), Motifs d'acides aminés (MeSH), Oomycetes (métabolisme), Oomycetes (pathogénicité), Phosphates phosphatidylinositol (métabolisme), Phytophthora infestans (métabolisme), Phytophthora infestans (pathogénicité), Solanum tuberosum (microbiologie), Séquence d'acides aminés (MeSH), Virulence (MeSH).
- MESH :
- microbiologie : Arabidopsis, Maladies des plantes, Solanum tuberosum.
- métabolisme : Facteurs de virulence, Lysine, Oomycetes, Phosphates phosphatidylinositol, Phytophthora infestans.
- pathogénicité : Oomycetes, Phytophthora infestans.
- Immunité des plantes, Motifs d'acides aminés, Séquence d'acides aminés, Virulence.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Arabidopsis (microbiology), Lysine (metabolism), Magnoliopsida (microbiology), Oomycetes (metabolism), Oomycetes (pathogenicity), Phosphatidylinositol Phosphates (metabolism), Phytophthora infestans (metabolism), Phytophthora infestans (pathogenicity), Plant Diseases (microbiology), Plant Immunity (MeSH), Solanum tuberosum (microbiology), Virulence (MeSH), Virulence Factors (metabolism).
- MESH :
- chemical , metabolism : Lysine, Phosphatidylinositol Phosphates, Virulence Factors.
- metabolism : Oomycetes, Phytophthora infestans.
- microbiology : Arabidopsis, Magnoliopsida, Plant Diseases, Solanum tuberosum.
- pathogenicity : Oomycetes, Phytophthora infestans.
- Amino Acid Motifs, Amino Acid Sequence, Plant Immunity, Virulence.
Abstract
The translocation of effector proteins into the host plant cells is essential for pathogens to suppress plant immune responses. The oomycete pathogen Phytophthora infestans secretes AVR3a, a crucial virulence effector protein with an N-terminal RXLR motif that is required for this translocation. It has been reported that the RXLR motif of P. sojae Avr1b, which is a close homolog of AVR3a, is required for binding to phosphatidylinositol monophosphates (PIPs). However, in our previous report, AVR3a as well as Avr1b bind to PIPs not via RXLR but via lysine residues forming a positively-charged area in the effector domain. In this report, we examined whether other RXLR effectors whose structures have been determined bind to PIPs. Both P. capsici AVR3a11 and Hyaloperonospora arabidopsidis ATR1 have an RXLR motif in their N-terminal regions but did not bind to any PIPs. These results suggest that the RXLR motif is not sufficient for PIP binding.
DOI: 10.4161/psb.23865
PubMed: 23425855
PubMed Central: PMC7030308
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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RIKEN; Tsurumi, Yokohama, Kanagawa, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Plant Science Center; RIKEN; Tsurumi, Yokohama, Kanagawa</wicri:regionArea><wicri:noRegion>Kanagawa</wicri:noRegion></affiliation></author><author><name sortKey="Shirasu, Ken" sort="Shirasu, Ken" uniqKey="Shirasu K" first="Ken" last="Shirasu">Ken Shirasu</name></author></analytic><series><title level="j">Plant signaling & behavior</title><idno type="eISSN">1559-2324</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Arabidopsis (microbiology)</term><term>Lysine (metabolism)</term><term>Magnoliopsida (microbiology)</term><term>Oomycetes (metabolism)</term><term>Oomycetes (pathogenicity)</term><term>Phosphatidylinositol Phosphates (metabolism)</term><term>Phytophthora infestans (metabolism)</term><term>Phytophthora infestans (pathogenicity)</term><term>Plant Diseases (microbiology)</term><term>Plant Immunity (MeSH)</term><term>Solanum tuberosum (microbiology)</term><term>Virulence (MeSH)</term><term>Virulence Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (microbiologie)</term><term>Facteurs de virulence (métabolisme)</term><term>Immunité des plantes (MeSH)</term><term>Lysine (métabolisme)</term><term>Maladies des plantes (microbiologie)</term><term>Motifs d'acides aminés (MeSH)</term><term>Oomycetes (métabolisme)</term><term>Oomycetes (pathogénicité)</term><term>Phosphates phosphatidylinositol (métabolisme)</term><term>Phytophthora infestans (métabolisme)</term><term>Phytophthora infestans (pathogénicité)</term><term>Solanum tuberosum (microbiologie)</term><term>Séquence d'acides aminés (MeSH)</term><term>Virulence (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lysine</term><term>Phosphatidylinositol Phosphates</term><term>Virulence Factors</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Oomycetes</term><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Arabidopsis</term><term>Maladies des plantes</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Arabidopsis</term><term>Magnoliopsida</term><term>Plant Diseases</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de virulence</term><term>Lysine</term><term>Oomycetes</term><term>Phosphates phosphatidylinositol</term><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Oomycetes</term><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Oomycetes</term><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Plant Immunity</term><term>Virulence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Immunité des plantes</term><term>Motifs d'acides aminés</term><term>Séquence d'acides aminés</term><term>Virulence</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The translocation of effector proteins into the host plant cells is essential for pathogens to suppress plant immune responses. The oomycete pathogen Phytophthora infestans secretes AVR3a, a crucial virulence effector protein with an N-terminal RXLR motif that is required for this translocation. It has been reported that the RXLR motif of P. sojae Avr1b, which is a close homolog of AVR3a, is required for binding to phosphatidylinositol monophosphates (PIPs). However, in our previous report, AVR3a as well as Avr1b bind to PIPs not via RXLR but via lysine residues forming a positively-charged area in the effector domain. In this report, we examined whether other RXLR effectors whose structures have been determined bind to PIPs. Both P. capsici AVR3a11 and Hyaloperonospora arabidopsidis ATR1 have an RXLR motif in their N-terminal regions but did not bind to any PIPs. These results suggest that the RXLR motif is not sufficient for PIP binding. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23425855</PMID><DateCompleted><Year>2014</Year><Month>06</Month><Day>09</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1559-2324</ISSN><JournalIssue CitedMedium="Internet"><Volume>8</Volume><Issue>4</Issue><PubDate><Year>2013</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Plant signaling & behavior</Title><ISOAbbreviation>Plant Signal Behav</ISOAbbreviation></Journal><ArticleTitle>The RXLR motif of oomycete effectors is not a sufficient element for binding to phosphatidylinositol monophosphates.</ArticleTitle><Pagination><MedlinePgn>e23865</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.4161/psb.23865</ELocationID><ELocationID EIdType="pii" ValidYN="Y">e23865</ELocationID><Abstract><AbstractText>The translocation of effector proteins into the host plant cells is essential for pathogens to suppress plant immune responses. The oomycete pathogen Phytophthora infestans secretes AVR3a, a crucial virulence effector protein with an N-terminal RXLR motif that is required for this translocation. It has been reported that the RXLR motif of P. sojae Avr1b, which is a close homolog of AVR3a, is required for binding to phosphatidylinositol monophosphates (PIPs). However, in our previous report, AVR3a as well as Avr1b bind to PIPs not via RXLR but via lysine residues forming a positively-charged area in the effector domain. In this report, we examined whether other RXLR effectors whose structures have been determined bind to PIPs. Both P. capsici AVR3a11 and Hyaloperonospora arabidopsidis ATR1 have an RXLR motif in their N-terminal regions but did not bind to any PIPs. These results suggest that the RXLR motif is not sufficient for PIP binding. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yaeno</LastName><ForeName>Takashi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Plant Science Center; RIKEN; Tsurumi, Yokohama, Kanagawa, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shirasu</LastName><ForeName>Ken</ForeName><Initials>K</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>2013</Year><Month>02</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Signal 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