A tomato LysM receptor‐like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB
Summary Resistance in tomato (Solanum lycopersicum) to infection by Pseudomonas syringae involves both detection of pathogen‐associated molecular patterns (PAMPs) and recognition by the host Pto kinase of pathogen effector AvrPtoB which is translocated into the host cell and interferes with PAMP‐tri...
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| creator | Zeng, Lirong Velásquez, André C. Munkvold, Kathy R. Zhang, Jingwei Martin, Gregory B. |
| description | Summary
Resistance in tomato (Solanum lycopersicum) to infection by Pseudomonas syringae involves both detection of pathogen‐associated molecular patterns (PAMPs) and recognition by the host Pto kinase of pathogen effector AvrPtoB which is translocated into the host cell and interferes with PAMP‐triggered immunity (PTI). The N‐terminal portion of AvrPtoB is sufficient for its virulence activity and for recognition by Pto. An amino acid substitution in AvrPtoB, F173A, abolishes these activities. To investigate the mechanisms of AvrPtoB virulence, we screened for tomato proteins that interact with AvrPtoB and identified Bti9, a LysM receptor‐like kinase. Bti9 has the highest amino acid similarity to Arabidopsis CERK1 among the tomato LysM receptor‐like kinases (RLKs) and belongs to a clade containing three other tomato proteins, SlLyk11, SlLyk12, and SlLyk13, all of which interact with AvrPtoB. The F173A substitution disrupts the interaction of AvrPtoB with Bti9 and SlLyk13, suggesting that these LysM‐RLKs are its virulence targets. Two independent tomato lines with RNAi‐mediated reduced expression of Bti9 and SlLyk13 were more susceptible to P. syringae. Bti9 kinase activity was inhibited in vitro by the N‐terminal domain of AvrPtoB in an F173‐dependent manner. These results indicate Bti9 and/or SlLyk13 play a role in plant immunity and the N‐terminal domain of AvrPtoB may have evolved to interfere with their kinase activity. Finally, we found that Bti9 and Pto interact with AvrPtoB in a structurally similar although not identical fashion, suggesting that Pto may have evolved as a molecular mimic of LysM‐RLK kinase domains. |
| doi_str_mv | 10.1111/j.1365-313X.2011.04773.x |
| format | Article |
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Resistance in tomato (Solanum lycopersicum) to infection by Pseudomonas syringae involves both detection of pathogen‐associated molecular patterns (PAMPs) and recognition by the host Pto kinase of pathogen effector AvrPtoB which is translocated into the host cell and interferes with PAMP‐triggered immunity (PTI). The N‐terminal portion of AvrPtoB is sufficient for its virulence activity and for recognition by Pto. An amino acid substitution in AvrPtoB, F173A, abolishes these activities. To investigate the mechanisms of AvrPtoB virulence, we screened for tomato proteins that interact with AvrPtoB and identified Bti9, a LysM receptor‐like kinase. Bti9 has the highest amino acid similarity to Arabidopsis CERK1 among the tomato LysM receptor‐like kinases (RLKs) and belongs to a clade containing three other tomato proteins, SlLyk11, SlLyk12, and SlLyk13, all of which interact with AvrPtoB. The F173A substitution disrupts the interaction of AvrPtoB with Bti9 and SlLyk13, suggesting that these LysM‐RLKs are its virulence targets. Two independent tomato lines with RNAi‐mediated reduced expression of Bti9 and SlLyk13 were more susceptible to P. syringae. Bti9 kinase activity was inhibited in vitro by the N‐terminal domain of AvrPtoB in an F173‐dependent manner. These results indicate Bti9 and/or SlLyk13 play a role in plant immunity and the N‐terminal domain of AvrPtoB may have evolved to interfere with their kinase activity. Finally, we found that Bti9 and Pto interact with AvrPtoB in a structurally similar although not identical fashion, suggesting that Pto may have evolved as a molecular mimic of LysM‐RLK kinase domains.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1111/j.1365-313X.2011.04773.x</identifier><identifier>PMID: 21880077</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Motifs ; Amino Acid Substitution ; amino acids ; Arabidopsis ; Arabidopsis Proteins ; Arabidopsis Proteins - chemistry ; AvrPtoB ; Bacterial Proteins ; Bacterial Proteins - metabolism ; Biological and medical sciences ; Cell receptors ; Cell structures and functions ; chemistry ; disease ; Fundamental and applied biological sciences. Psychology ; genetics ; Host-Pathogen Interactions ; hosts ; Immunity ; immunology ; Infection ; Kinases ; Lycopersicon esculentum ; Lycopersicon esculentum - genetics ; Lycopersicon esculentum - immunology ; Lycopersicon esculentum - metabolism ; Lycopersicon esculentum - microbiology ; metabolism ; microbiology ; Miscellaneous ; Molecular and cellular biology ; Molecular Mimicry ; Molecular Sequence Data ; PAMP‐triggered immunity ; pathogenicity ; Pathogens ; phosphotransferases (kinases) ; Plant biology ; Plant pathology ; Plant physiology and development ; Plant Proteins ; Plant Proteins - chemistry ; Plant Proteins - immunology ; Plant Proteins - metabolism ; Plant resistance ; Plants, Genetically Modified ; Protein Serine-Threonine Kinases ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - immunology ; Protein-Serine-Threonine Kinases - metabolism ; proteins ; Pseudomonas syringae ; Pseudomonas syringae - pathogenicity ; Pto kinase ; Solanum ; Solanum lycopersicum ; tomato ; Tomatoes ; Two-Hybrid System Techniques ; Virulence</subject><ispartof>The Plant journal : for cell and molecular biology, 2012-01, Vol.69 (1), p.92-103</ispartof><rights>2011 The Authors. The Plant Journal © 2011 Blackwell Publishing Ltd</rights><rights>2015 INIST-CNRS</rights><rights>2011 The Authors. The Plant Journal © 2011 Blackwell Publishing Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6623-60968083715485f953efa9d44dd71c5bc47e8ad98cde95d8b14f2c52bf0f8b543</citedby><cites>FETCH-LOGICAL-c6623-60968083715485f953efa9d44dd71c5bc47e8ad98cde95d8b14f2c52bf0f8b543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-313X.2011.04773.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-313X.2011.04773.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25349949$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21880077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zeng, Lirong</creatorcontrib><creatorcontrib>Velásquez, André C.</creatorcontrib><creatorcontrib>Munkvold, Kathy R.</creatorcontrib><creatorcontrib>Zhang, Jingwei</creatorcontrib><creatorcontrib>Martin, Gregory B.</creatorcontrib><title>A tomato LysM receptor‐like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB</title><title>The Plant journal : for cell and molecular biology</title><addtitle>Plant J</addtitle><description>Summary
Resistance in tomato (Solanum lycopersicum) to infection by Pseudomonas syringae involves both detection of pathogen‐associated molecular patterns (PAMPs) and recognition by the host Pto kinase of pathogen effector AvrPtoB which is translocated into the host cell and interferes with PAMP‐triggered immunity (PTI). The N‐terminal portion of AvrPtoB is sufficient for its virulence activity and for recognition by Pto. An amino acid substitution in AvrPtoB, F173A, abolishes these activities. To investigate the mechanisms of AvrPtoB virulence, we screened for tomato proteins that interact with AvrPtoB and identified Bti9, a LysM receptor‐like kinase. Bti9 has the highest amino acid similarity to Arabidopsis CERK1 among the tomato LysM receptor‐like kinases (RLKs) and belongs to a clade containing three other tomato proteins, SlLyk11, SlLyk12, and SlLyk13, all of which interact with AvrPtoB. The F173A substitution disrupts the interaction of AvrPtoB with Bti9 and SlLyk13, suggesting that these LysM‐RLKs are its virulence targets. Two independent tomato lines with RNAi‐mediated reduced expression of Bti9 and SlLyk13 were more susceptible to P. syringae. Bti9 kinase activity was inhibited in vitro by the N‐terminal domain of AvrPtoB in an F173‐dependent manner. These results indicate Bti9 and/or SlLyk13 play a role in plant immunity and the N‐terminal domain of AvrPtoB may have evolved to interfere with their kinase activity. Finally, we found that Bti9 and Pto interact with AvrPtoB in a structurally similar although not identical fashion, suggesting that Pto may have evolved as a molecular mimic of LysM‐RLK kinase domains.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Substitution</subject><subject>amino acids</subject><subject>Arabidopsis</subject><subject>Arabidopsis Proteins</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>AvrPtoB</subject><subject>Bacterial Proteins</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>chemistry</subject><subject>disease</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genetics</subject><subject>Host-Pathogen Interactions</subject><subject>hosts</subject><subject>Immunity</subject><subject>immunology</subject><subject>Infection</subject><subject>Kinases</subject><subject>Lycopersicon esculentum</subject><subject>Lycopersicon esculentum - genetics</subject><subject>Lycopersicon esculentum - immunology</subject><subject>Lycopersicon esculentum - metabolism</subject><subject>Lycopersicon esculentum - microbiology</subject><subject>metabolism</subject><subject>microbiology</subject><subject>Miscellaneous</subject><subject>Molecular and cellular biology</subject><subject>Molecular Mimicry</subject><subject>Molecular Sequence Data</subject><subject>PAMP‐triggered immunity</subject><subject>pathogenicity</subject><subject>Pathogens</subject><subject>phosphotransferases (kinases)</subject><subject>Plant biology</subject><subject>Plant pathology</subject><subject>Plant physiology and development</subject><subject>Plant Proteins</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - immunology</subject><subject>Plant Proteins - metabolism</subject><subject>Plant resistance</subject><subject>Plants, Genetically Modified</subject><subject>Protein Serine-Threonine Kinases</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - immunology</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>proteins</subject><subject>Pseudomonas syringae</subject><subject>Pseudomonas syringae - pathogenicity</subject><subject>Pto kinase</subject><subject>Solanum</subject><subject>Solanum lycopersicum</subject><subject>tomato</subject><subject>Tomatoes</subject><subject>Two-Hybrid System Techniques</subject><subject>Virulence</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc2O0zAUhS0EYkrhFZCFhMQmwY6d2F6AVEb8qohZDBI7y3Ecxp0k7thOmex4BJ6RJ8GhnfKzAW9s-X736px7AIAY5Tidp5sck6rMCCaf8gJhnCPKGMmvb4HFsXAbLJCoUMYoLk7AvRA2CGFGKnoXnBSYc4QYW4B2BaPrVXRwPYX30BttttH571-_dfbSwEs7qGDg1rveRROg7ftxsHGCamigjeEGUDra3fxvEzNc2NpG08B6gqudP4vuxX1wp1VdMA8O9xJ8fPXy_PRNtv7w-u3pap3pqipIViXFHHHCcEl52YqSmFaJhtKmYViXtabMcNUIrhsjyobXmLaFLou6RS2vS0qW4Pl-7nase9NoM0SvOrn1tld-kk5Z-WdlsBfys9tJUlDE0DzgyWGAd1ejCVH2NmjTdWowbgwS07RFgjHh_0ZRkawIwWb00V_oxo1-SJuQAhcElSi5XwK-h7R3IXjTHmVjJOfY5UbO6co5XTnHLn_GLq9T68PfbR8bb3JOwOMDoIJWXevVoG34xZWECkFF4p7tuS-2M9N_C5DnZ-_mF_kBprPKiA</recordid><startdate>201201</startdate><enddate>201201</enddate><creator>Zeng, Lirong</creator><creator>Velásquez, André C.</creator><creator>Munkvold, Kathy R.</creator><creator>Zhang, Jingwei</creator><creator>Martin, Gregory B.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7T5</scope><scope>H94</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>201201</creationdate><title>A tomato LysM receptor‐like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB</title><author>Zeng, Lirong ; Velásquez, André C. ; Munkvold, Kathy R. ; Zhang, Jingwei ; Martin, Gregory B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6623-60968083715485f953efa9d44dd71c5bc47e8ad98cde95d8b14f2c52bf0f8b543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Substitution</topic><topic>amino acids</topic><topic>Arabidopsis</topic><topic>Arabidopsis Proteins</topic><topic>Arabidopsis Proteins - chemistry</topic><topic>AvrPtoB</topic><topic>Bacterial Proteins</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>chemistry</topic><topic>disease</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genetics</topic><topic>Host-Pathogen Interactions</topic><topic>hosts</topic><topic>Immunity</topic><topic>immunology</topic><topic>Infection</topic><topic>Kinases</topic><topic>Lycopersicon esculentum</topic><topic>Lycopersicon esculentum - genetics</topic><topic>Lycopersicon esculentum - immunology</topic><topic>Lycopersicon esculentum - metabolism</topic><topic>Lycopersicon esculentum - microbiology</topic><topic>metabolism</topic><topic>microbiology</topic><topic>Miscellaneous</topic><topic>Molecular and cellular biology</topic><topic>Molecular Mimicry</topic><topic>Molecular Sequence Data</topic><topic>PAMP‐triggered immunity</topic><topic>pathogenicity</topic><topic>Pathogens</topic><topic>phosphotransferases (kinases)</topic><topic>Plant biology</topic><topic>Plant pathology</topic><topic>Plant physiology and development</topic><topic>Plant Proteins</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - immunology</topic><topic>Plant Proteins - metabolism</topic><topic>Plant resistance</topic><topic>Plants, Genetically Modified</topic><topic>Protein Serine-Threonine Kinases</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - immunology</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>proteins</topic><topic>Pseudomonas syringae</topic><topic>Pseudomonas syringae - pathogenicity</topic><topic>Pto kinase</topic><topic>Solanum</topic><topic>Solanum lycopersicum</topic><topic>tomato</topic><topic>Tomatoes</topic><topic>Two-Hybrid System Techniques</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zeng, Lirong</creatorcontrib><creatorcontrib>Velásquez, André C.</creatorcontrib><creatorcontrib>Munkvold, Kathy R.</creatorcontrib><creatorcontrib>Zhang, Jingwei</creatorcontrib><creatorcontrib>Martin, Gregory B.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Plant journal : for cell and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zeng, Lirong</au><au>Velásquez, André C.</au><au>Munkvold, Kathy R.</au><au>Zhang, Jingwei</au><au>Martin, Gregory B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A tomato LysM receptor‐like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB</atitle><jtitle>The Plant journal : for cell and molecular biology</jtitle><addtitle>Plant J</addtitle><date>2012-01</date><risdate>2012</risdate><volume>69</volume><issue>1</issue><spage>92</spage><epage>103</epage><pages>92-103</pages><issn>0960-7412</issn><eissn>1365-313X</eissn><abstract>Summary
Resistance in tomato (Solanum lycopersicum) to infection by Pseudomonas syringae involves both detection of pathogen‐associated molecular patterns (PAMPs) and recognition by the host Pto kinase of pathogen effector AvrPtoB which is translocated into the host cell and interferes with PAMP‐triggered immunity (PTI). The N‐terminal portion of AvrPtoB is sufficient for its virulence activity and for recognition by Pto. An amino acid substitution in AvrPtoB, F173A, abolishes these activities. To investigate the mechanisms of AvrPtoB virulence, we screened for tomato proteins that interact with AvrPtoB and identified Bti9, a LysM receptor‐like kinase. Bti9 has the highest amino acid similarity to Arabidopsis CERK1 among the tomato LysM receptor‐like kinases (RLKs) and belongs to a clade containing three other tomato proteins, SlLyk11, SlLyk12, and SlLyk13, all of which interact with AvrPtoB. The F173A substitution disrupts the interaction of AvrPtoB with Bti9 and SlLyk13, suggesting that these LysM‐RLKs are its virulence targets. Two independent tomato lines with RNAi‐mediated reduced expression of Bti9 and SlLyk13 were more susceptible to P. syringae. Bti9 kinase activity was inhibited in vitro by the N‐terminal domain of AvrPtoB in an F173‐dependent manner. These results indicate Bti9 and/or SlLyk13 play a role in plant immunity and the N‐terminal domain of AvrPtoB may have evolved to interfere with their kinase activity. Finally, we found that Bti9 and Pto interact with AvrPtoB in a structurally similar although not identical fashion, suggesting that Pto may have evolved as a molecular mimic of LysM‐RLK kinase domains.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>21880077</pmid><doi>10.1111/j.1365-313X.2011.04773.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; IngentaConnect Free/Open Access Journals; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Motifs Amino Acid Substitution amino acids Arabidopsis Arabidopsis Proteins Arabidopsis Proteins - chemistry AvrPtoB Bacterial Proteins Bacterial Proteins - metabolism Biological and medical sciences Cell receptors Cell structures and functions chemistry disease Fundamental and applied biological sciences. Psychology genetics Host-Pathogen Interactions hosts Immunity immunology Infection Kinases Lycopersicon esculentum Lycopersicon esculentum - genetics Lycopersicon esculentum - immunology Lycopersicon esculentum - metabolism Lycopersicon esculentum - microbiology metabolism microbiology Miscellaneous Molecular and cellular biology Molecular Mimicry Molecular Sequence Data PAMP‐triggered immunity pathogenicity Pathogens phosphotransferases (kinases) Plant biology Plant pathology Plant physiology and development Plant Proteins Plant Proteins - chemistry Plant Proteins - immunology Plant Proteins - metabolism Plant resistance Plants, Genetically Modified Protein Serine-Threonine Kinases Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - immunology Protein-Serine-Threonine Kinases - metabolism proteins Pseudomonas syringae Pseudomonas syringae - pathogenicity Pto kinase Solanum Solanum lycopersicum tomato Tomatoes Two-Hybrid System Techniques Virulence |
| title | A tomato LysM receptor‐like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB |
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