Autoacetylation of the Ralstonia solanacearum Effector PopP2 Targets a Lysine Residue Essential for RRS1-R-Mediated Immunity in Arabidopsis
Type III effector proteins from bacterial pathogens manipulate components of host immunity to suppress defence responses and promote pathogen development. In plants, host proteins targeted by some effectors called avirulence proteins are surveyed by plant disease resistance proteins referred to as &...
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| Published in | PLoS pathogens Vol. 6; no. 11; p. e1001202 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Public Library of Science
18.11.2010
Public Library of Science (PLoS) |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1553-7374 1553-7366 1553-7374 |
| DOI | 10.1371/journal.ppat.1001202 |
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| Abstract | Type III effector proteins from bacterial pathogens manipulate components of host immunity to suppress defence responses and promote pathogen development. In plants, host proteins targeted by some effectors called avirulence proteins are surveyed by plant disease resistance proteins referred to as "guards". The Ralstonia solanacearum effector protein PopP2 triggers immunity in Arabidopsis following its perception by the RRS1-R resistance protein. Here, we show that PopP2 interacts with RRS1-R in the nucleus of living plant cells. PopP2 belongs to the YopJ-like family of cysteine proteases, which share a conserved catalytic triad that includes a highly conserved cysteine residue. The catalytic cysteine mutant PopP2-C321A is impaired in its avirulence activity although it is still able to interact with RRS1-R. In addition, PopP2 prevents proteasomal degradation of RRS1-R, independent of the presence of an integral PopP2 catalytic core. A liquid chromatography/tandem mass spectrometry analysis showed that PopP2 displays acetyl-transferase activity leading to its autoacetylation on a particular lysine residue, which is well conserved among all members of the YopJ family. These data suggest that this lysine residue may correspond to a key binding site for acetyl-coenzyme A required for protein activity. Indeed, mutation of this lysine in PopP2 abolishes RRS1-R-mediated immunity. In agreement with the guard hypothesis, our results favour the idea that activation of the plant immune response by RRS1-R depends not only on the physical interaction between the two proteins but also on its perception of PopP2 enzymatic activity. |
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| AbstractList | Type III effector proteins from bacterial pathogens manipulate components of host immunity to suppress defence responses and promote pathogen development. In plants, host proteins targeted by some effectors called avirulence proteins are surveyed by plant disease resistance proteins referred to as "guards". The Ralstonia solanacearum effector protein PopP2 triggers immunity in Arabidopsis following its perception by the RRS1-R resistance protein. Here, we show that PopP2 interacts with RRS1-R in the nucleus of living plant cells. PopP2 belongs to the YopJ-like family of cysteine proteases, which share a conserved catalytic triad that includes a highly conserved cysteine residue. The catalytic cysteine mutant PopP2-C321A is impaired in its avirulence activity although it is still able to interact with RRS1-R. In addition, PopP2 prevents proteasomal degradation of RRS1-R, independent of the presence of an integral PopP2 catalytic core. A liquid chromatography/tandem mass spectrometry analysis showed that PopP2 displays acetyl-transferase activity leading to its autoacetylation on a particular lysine residue, which is well conserved among all members of the YopJ family. These data suggest that this lysine residue may correspond to a key binding site for acetyl-coenzyme A required for protein activity. Indeed, mutation of this lysine in PopP2 abolishes RRS1-R-mediated immunity. In agreement with the guard hypothesis, our results favour the idea that activation of the plant immune response by RRS1-R depends not only on the physical interaction between the two proteins but also on its perception of PopP2 enzymatic activity. Plant and animal bacterial pathogens have evolved to produce virulence factors, called type III effectors, which are injected into host cells to suppress host defences and provide an environment beneficial for pathogen growth. Type III effectors from pathogenic bacteria display enzymatic activities, often mimicking an endogenous eukaryotic activity, to target host signalling pathways. Elucidation of strategies used by pathogens to manipulate host protein activities is a subject of fundamental interest in pathology. PopP2 is a YopJ-like effector from the soil borne root pathogen Ralstonia solanacearum. Here, in addition to demonstrating PopP2 ability to stabilize the expression of its cognate Arabidopsis RRS1-R resistance protein and physically interact with it, we investigated the enzymatic activity of PopP2. Bacterial YopJ-like effectors are predicted to act as acetyl-transferases on host components. However, only two YopJ-like proteins from animal pathogens have been shown to be active acetyl-transferases. We show that PopP2 displays autoacetyl-transferase activity targeting a lysine residue well-conserved among YopJ-like family members. This lysine is a critical residue since its mutation prevents autoacetylation of PopP2 and abolishes its recognition by the host. This study provides new clues on the multiple properties displayed by bacterial type III effectors that may be used to target defense-related host components. Type III effector proteins from bacterial pathogens manipulate components of host immunity to suppress defence responses and promote pathogen development. In plants, host proteins targeted by some effectors called avirulence proteins are surveyed by plant disease resistance proteins referred to as "guards". The Ralstonia solanacearum effector protein PopP2 triggers immunity in Arabidopsis following its perception by the RRS1-R resistance protein. Here, we show that PopP2 interacts with RRS1-R in the nucleus of living plant cells. PopP2 belongs to the YopJ-like family of cysteine proteases, which share a conserved catalytic triad that includes a highly conserved cysteine residue. The catalytic cysteine mutant PopP2-C321A is impaired in its avirulence activity although it is still able to interact with RRS1-R. In addition, PopP2 prevents proteasomal degradation of RRS1-R, independent of the presence of an integral PopP2 catalytic core. A liquid chromatography/tandem mass spectrometry analysis showed that PopP2 displays acetyl-transferase activity leading to its autoacetylation on a particular lysine residue, which is well conserved among all members of the YopJ family. These data suggest that this lysine residue may correspond to a key binding site for acetyl-coenzyme A required for protein activity. Indeed, mutation of this lysine in PopP2 abolishes RRS1-R-mediated immunity. In agreement with the guard hypothesis, our results favour the idea that activation of the plant immune response by RRS1-R depends not only on the physical interaction between the two proteins but also on its perception of PopP2 enzymatic activity. Type III effector proteins from bacterial pathogens manipulate components of host immunity to suppress defence responses and promote pathogen development. In plants, host proteins targeted by some effectors called avirulence proteins are surveyed by plant disease resistance proteins referred to as "guards". The Ralstonia solanacearum effector protein PopP2 triggers immunity in Arabidopsis following its perception by the RRS1-R resistance protein. Here, we show that PopP2 interacts with RRS1-R in the nucleus of living plant cells. PopP2 belongs to the YopJ-like family of cysteine proteases, which share a conserved catalytic triad that includes a highly conserved cysteine residue. The catalytic cysteine mutant PopP2-C321A is impaired in its avirulence activity although it is still able to interact with RRS1-R. In addition, PopP2 prevents proteasomal degradation of RRS1-R, independent of the presence of an integral PopP2 catalytic core. A liquid chromatography/tandem mass spectrometry analysis showed that PopP2 displays acetyl-transferase activity leading to its autoacetylation on a particular lysine residue, which is well conserved among all members of the YopJ family. These data suggest that this lysine residue may correspond to a key binding site for acetyl-coenzyme A required for protein activity. Indeed, mutation of this lysine in PopP2 abolishes RRS1-R-mediated immunity. In agreement with the guard hypothesis, our results favour the idea that activation of the plant immune response by RRS1-R depends not only on the physical interaction between the two proteins but also on its perception of PopP2 enzymatic activity.Type III effector proteins from bacterial pathogens manipulate components of host immunity to suppress defence responses and promote pathogen development. In plants, host proteins targeted by some effectors called avirulence proteins are surveyed by plant disease resistance proteins referred to as "guards". The Ralstonia solanacearum effector protein PopP2 triggers immunity in Arabidopsis following its perception by the RRS1-R resistance protein. Here, we show that PopP2 interacts with RRS1-R in the nucleus of living plant cells. PopP2 belongs to the YopJ-like family of cysteine proteases, which share a conserved catalytic triad that includes a highly conserved cysteine residue. The catalytic cysteine mutant PopP2-C321A is impaired in its avirulence activity although it is still able to interact with RRS1-R. In addition, PopP2 prevents proteasomal degradation of RRS1-R, independent of the presence of an integral PopP2 catalytic core. A liquid chromatography/tandem mass spectrometry analysis showed that PopP2 displays acetyl-transferase activity leading to its autoacetylation on a particular lysine residue, which is well conserved among all members of the YopJ family. These data suggest that this lysine residue may correspond to a key binding site for acetyl-coenzyme A required for protein activity. Indeed, mutation of this lysine in PopP2 abolishes RRS1-R-mediated immunity. In agreement with the guard hypothesis, our results favour the idea that activation of the plant immune response by RRS1-R depends not only on the physical interaction between the two proteins but also on its perception of PopP2 enzymatic activity. Type III effector proteins from bacterial pathogens manipulate components of host immunity to suppress defence responses and promote pathogen development. In plants, host proteins targeted by some effectors called avirulence proteins are surveyed by plant disease resistance proteins referred to as “guards”. The Ralstonia solanacearum effector protein PopP2 triggers immunity in Arabidopsis following its perception by the RRS1-R resistance protein. Here, we show that PopP2 interacts with RRS1-R in the nucleus of living plant cells. PopP2 belongs to the YopJ-like family of cysteine proteases, which share a conserved catalytic triad that includes a highly conserved cysteine residue. The catalytic cysteine mutant PopP2-C321A is impaired in its avirulence activity although it is still able to interact with RRS1-R. In addition, PopP2 prevents proteasomal degradation of RRS1-R, independent of the presence of an integral PopP2 catalytic core. A liquid chromatography/tandem mass spectrometry analysis showed that PopP2 displays acetyl-transferase activity leading to its autoacetylation on a particular lysine residue, which is well conserved among all members of the YopJ family. These data suggest that this lysine residue may correspond to a key binding site for acetyl-coenzyme A required for protein activity. Indeed, mutation of this lysine in PopP2 abolishes RRS1-R-mediated immunity. In agreement with the guard hypothesis, our results favour the idea that activation of the plant immune response by RRS1-R depends not only on the physical interaction between the two proteins but also on its perception of PopP2 enzymatic activity. Plant and animal bacterial pathogens have evolved to produce virulence factors, called type III effectors, which are injected into host cells to suppress host defences and provide an environment beneficial for pathogen growth. Type III effectors from pathogenic bacteria display enzymatic activities, often mimicking an endogenous eukaryotic activity, to target host signalling pathways. Elucidation of strategies used by pathogens to manipulate host protein activities is a subject of fundamental interest in pathology. PopP2 is a YopJ-like effector from the soil borne root pathogen Ralstonia solanacearum. Here, in addition to demonstrating PopP2 ability to stabilize the expression of its cognate Arabidopsis RRS1-R resistance protein and physically interact with it, we investigated the enzymatic activity of PopP2. Bacterial YopJ-like effectors are predicted to act as acetyl-transferases on host components. However, only two YopJ-like proteins from animal pathogens have been shown to be active acetyl-transferases. We show that PopP2 displays autoacetyl-transferase activity targeting a lysine residue well-conserved among YopJ-like family members. This lysine is a critical residue since its mutation prevents autoacetylation of PopP2 and abolishes its recognition by the host. This study provides new clues on the multiple properties displayed by bacterial type III effectors that may be used to target defense-related host components. Type III effector proteins from bacterial pathogens manipulate components of host immunity to suppress defence responses and promote pathogen development. In plants, host proteins targeted by some effectors called avirulence proteins are surveyed by plant disease resistance proteins referred to as "guards". The Ralstonia solanacearum effector protein PopP2 triggers immunity in Arabidopsis following its perception by the RRS1-R resistance protein. Here, we show that PopP2 interacts with RRS1-R in the nucleus of living plant cells. PopP2 belongs to the YopJ-like family of cysteine proteases, which share a conserved catalytic triad that includes a highly conserved cysteine residue. The catalytic cysteine mutant PopP2-C321A is impaired in its avirulence activity although it is still able to interact with RRS1-R. In addition, PopP2 prevents proteasomal degradation of RRS1-R, independent of the presence of an integral PopP2 catalytic core. A liquid chromatography/tandem mass spectrometry analysis showed that PopP2 displays acetyl-transferase activity leading to its autoacetylation on a particular lysine residue, which is well conserved among all members of the YopJ family. These data suggest that this lysine residue may correspond to a key binding site for acetyl-coenzyme A required for protein activity. Indeed, mutation of this lysine in PopP2 abolishes RRS1-R-mediated immunity. In agreement with the guard hypothesis, our results favour the idea that activation of the plant immune response by RRS1-R depends not only on the physical interaction between the two proteins but also on its perception of PopP2 enzymatic activity. |
| Audience | Academic |
| Author | Jauneau, Alain Kieffer-Jacquinod, Sylvie Pouzet, Cécile Deslandes, Laurent Bernoux, Maud Marco, Yves Brière, Christian Rivas, Susana Tasset, Céline |
| AuthorAffiliation | 3 Surfaces Cellulaires et Signalisation chez les Végétaux, Université de Toulouse, UMR CNRS-Université Paul Sabatier 5546, Castanet-Tolosan, France 2 Institut Fédératif de Recherche 40, Plateforme Imagerie, Pôle de Biotechnologie Végétale, Castanet-Tolosan, France The University of North Carolina at Chapel Hill, United States of America 1 Laboratoire des Interactions Plantes Microorganismes (LIPM), UMR CNRS-INRA 2594/441, Castanet-Tolosan, France 4 CEA, DSV/IRTSV Laboratoire EdyP, Grenoble, France |
| AuthorAffiliation_xml | – name: 4 CEA, DSV/IRTSV Laboratoire EdyP, Grenoble, France – name: 1 Laboratoire des Interactions Plantes Microorganismes (LIPM), UMR CNRS-INRA 2594/441, Castanet-Tolosan, France – name: 3 Surfaces Cellulaires et Signalisation chez les Végétaux, Université de Toulouse, UMR CNRS-Université Paul Sabatier 5546, Castanet-Tolosan, France – name: The University of North Carolina at Chapel Hill, United States of America – name: 2 Institut Fédératif de Recherche 40, Plateforme Imagerie, Pôle de Biotechnologie Végétale, Castanet-Tolosan, France |
| Author_xml | – sequence: 1 givenname: Céline surname: Tasset fullname: Tasset, Céline – sequence: 2 givenname: Maud surname: Bernoux fullname: Bernoux, Maud – sequence: 3 givenname: Alain surname: Jauneau fullname: Jauneau, Alain – sequence: 4 givenname: Cécile surname: Pouzet fullname: Pouzet, Cécile – sequence: 5 givenname: Christian surname: Brière fullname: Brière, Christian – sequence: 6 givenname: Sylvie surname: Kieffer-Jacquinod fullname: Kieffer-Jacquinod, Sylvie – sequence: 7 givenname: Susana surname: Rivas fullname: Rivas, Susana – sequence: 8 givenname: Yves surname: Marco fullname: Marco, Yves – sequence: 9 givenname: Laurent surname: Deslandes fullname: Deslandes, Laurent |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21124938$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1126/science.1126867 10.1074/jbc.M706970200 10.1038/nature05966 10.1126/science.1129523 10.1046/j.1365-2958.2003.03588.x 10.1016/S0955-0674(03)00003-6 10.1093/emboj/19.15.4004 10.1105/tpc.108.058685 10.1073/pnas.0602577103 10.1111/j.1365-313X.2008.03596.x 10.1038/nature04946 10.1016/S0968-0004(98)01311-5 10.1146/annurev.ge.24.120190.002311 10.1126/science.1111404 10.1105/tpc.107.056325 10.1016/j.pbi.2008.06.007 10.1016/j.chom.2007.03.006 10.1094/MPMI-22-5-0538 10.1073/pnas.0608779104 10.1111/j.1462-5822.2007.00990.x 10.1105/tpc.104.024141 10.1016/S0092-8674(01)00619-5 10.1016/j.str.2005.01.020 10.1105/tpc.108.058529 10.1016/j.cell.2005.03.025 10.1073/pnas.032485099 10.1007/s11103-005-5817-8 10.1016/S1097-2765(03)00528-8 10.1016/S0092-8674(02)00661-X 10.1146/annurev.py.29.090191.000433 10.1046/j.1365-2958.2003.03666.x 10.1016/S0021-9258(18)54150-8 10.1093/nar/gkj089 10.1146/annurev.arplant.57.032905.105346 10.1038/35081161 10.1016/j.cub.2007.12.020 10.1126/science.274.5295.2063 10.1038/nature05286 10.1038/nature06109 10.1016/S0092-8674(03)00040-0 10.1126/science.1144958 10.1111/j.1365-2958.2004.04118.x 10.1038/nature03630 10.1046/j.1365-2958.2003.03730.x 10.1111/j.1365-313X.2005.02500.x 10.1038/nrm1984 10.1074/jbc.M505294200 10.1016/j.cell.2006.02.008 10.1016/S0092-8674(03)00036-9 10.1126/science.1171647 10.1126/science.1144956 10.1016/j.semcdb.2009.04.010 10.1046/j.1365-2958.2003.03616.x 10.1073/pnas.1230660100 10.1073/pnas.0500792102 10.1126/science.1085671 10.1016/j.pbi.2007.04.020 10.1016/j.pbi.2004.05.003 10.1094/MPMI.1998.11.7.659 10.1094/MPMI.2004.17.6.633 10.1073/pnas.0608995103 10.1016/j.tibs.2007.03.007 10.1038/nature05737 10.1016/S0959-437X(99)80022-7 |
| ContentType | Journal Article |
| Copyright | COPYRIGHT 2010 Public Library of Science Tasset et al. 2010 2010 Tasset et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Tasset C, Bernoux M, Jauneau A, Pouzet C, Brière C, et al. (2010) Autoacetylation of the Ralstonia solanacearum Effector PopP2 Targets a Lysine Residue Essential for RRS1-R-Mediated Immunity in Arabidopsis. PLoS Pathog 6(11): e1001202. doi:10.1371/journal.ppat.1001202 |
| Copyright_xml | – notice: COPYRIGHT 2010 Public Library of Science – notice: Tasset et al. 2010 – notice: 2010 Tasset et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Tasset C, Bernoux M, Jauneau A, Pouzet C, Brière C, et al. (2010) Autoacetylation of the Ralstonia solanacearum Effector PopP2 Targets a Lysine Residue Essential for RRS1-R-Mediated Immunity in Arabidopsis. PLoS Pathog 6(11): e1001202. doi:10.1371/journal.ppat.1001202 |
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| DOI | 10.1371/journal.ppat.1001202 |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 Conceived and designed the experiments: CT LD. Performed the experiments: CT MB AJ CP CB SKJ LD. Analyzed the data: CT SR YM LD. Contributed reagents/materials/analysis tools: CT LD. Wrote the paper: CT SR YM LD. Current address: CSIRO Plant Industry, Canberra, Australian Capital Territory, Australia |
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| References | SR Scofield (ref7) 1996; 274 F Shao (ref20) 2003; 301 K Gu (ref27) 2005; 435 ND Rawlings (ref41) 2006; 34 S Mukherjee (ref44) 2006; 312 E Meylan (ref5) 2006; 442 M Bernoux (ref46) 2008; 20 I Lassot (ref56) 2005; 280 CR Sweet (ref55) 2007; 9 MJ Axtell (ref21) 2003; 112 L Deslandes (ref9) 2003; 100 JR Bretz (ref32) 2003; 49 M Rafiqi (ref3) 2009; 20 W Xing (ref30) 2007; 449 L Deslandes (ref38) 2002; 99 A Friedler (ref63) 2005; 13 T Eulgem (ref36) 2007; 10 MJ Axtell (ref54) 2003; 49 JG Kim (ref65) 2008; 20 D Mackey (ref14) 2003; 112 T Xiang (ref29) 2008; 18 JE Trosky (ref47) 2007; 282 Y Jia (ref8) 2000; 19 J Marion (ref66) 2008; 56 Y Noutoshi (ref57) 2005; 43 T Boller (ref2) 2009; 60 A Espinosa (ref33) 2003; 49 KV Krasileva (ref10) 2010 JD Jones (ref1) 2006; 444 J Ade (ref16) 2007; 104 NT Keen (ref50) 1990; 24 A Block (ref19) 2008; 11 S Kay (ref25) 2007; 318 P Romer (ref26) 2007; 318 ST Chisholm (ref4) 2006; 124 HC Rooney (ref15) 2005; 308 L Deslandes (ref37) 1998; 11 M Shabab (ref18) 2008; 20 EA Van der Biezen (ref11) 1998; 23 L Hong (ref60) 1993; 268 M Poueymiro (ref67) 2009; 22 AJ Wu (ref31) 2004; 16 S Cunnac (ref48) 2004; 53 D Mackey (ref13) 2002; 108 PN Dodds (ref51) 2006; 103 J Roden (ref42) 2004; 17 J Zhang (ref34) 2007; 1 A Hotson (ref39) 2003; 50 H Ueda (ref52) 2006; 61 ZQ Fu (ref28) 2007; 447 C Prives (ref62) 2001; 107 TR Rosebrock (ref23) 2007; 448 G Vidali (ref58) 1968; 243 A Hotson (ref40) 2004; 7 MG Kim (ref17) 2005; 121 CL Brooks (ref61) 2003; 15 K Nomura (ref24) 2006; 313 S Mukherjee (ref45) 2007; 32 S Mujtaba (ref64) 2004; 13 HS Kim (ref53) 2005; 102 Flor (ref49) 1971; 9 RB Abramovitch (ref22) 2006; 7 AC Hayward (ref35) 1991; 29 T Boller (ref6) 2009; 324 RD Kornberg (ref59) 1999; 9 JL Dangl (ref12) 2001; 411 R Mittal (ref43) 2006; 103 35235614 - PLoS Pathog. 2022 Mar 2;18(3):e1010368 |
| References_xml | – volume: 312 start-page: 1211 year: 2006 ident: ref44 article-title: Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. publication-title: Science doi: 10.1126/science.1126867 – volume: 282 start-page: 34299 year: 2007 ident: ref47 article-title: VopA inhibits ATP binding by acetylating the catalytic loop of MAPK kinases. publication-title: J Biol Chem doi: 10.1074/jbc.M706970200 – volume: 448 start-page: 370 year: 2007 ident: ref23 article-title: A bacterial E3 ubiquitin ligase targets a host protein kinase to disrupt plant immunity. publication-title: Nature doi: 10.1038/nature05966 – volume: 313 start-page: 220 year: 2006 ident: ref24 article-title: A bacterial virulence protein suppresses host innate immunity to cause plant disease. publication-title: Science doi: 10.1126/science.1129523 – volume: 49 start-page: 377 year: 2003 ident: ref33 article-title: The Pseudomonas syringae type III-secreted protein HopPtoD2 possesses protein tyrosine phosphatase activity and suppresses programmed cell death in plants. publication-title: Mol Microbiol doi: 10.1046/j.1365-2958.2003.03588.x – volume: 15 start-page: 164 year: 2003 ident: ref61 article-title: Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. publication-title: Curr Opin Cell Biol doi: 10.1016/S0955-0674(03)00003-6 – volume: 19 start-page: 4004 year: 2000 ident: ref8 article-title: Direct interaction of resistance gene and avirulence gene products confers rice blast resistance. publication-title: Embo J doi: 10.1093/emboj/19.15.4004 – volume: 20 start-page: 2252 year: 2008 ident: ref46 article-title: RD19, an Arabidopsis cysteine protease required for RRS1-R-mediated resistance, is relocalized to the nucleus by the Ralstonia solanacearum PopP2 effector. publication-title: Plant Cell doi: 10.1105/tpc.108.058685 – volume: 103 start-page: 8888 year: 2006 ident: ref51 article-title: Direct protein interaction underlies gene-for-gene specificity and coevolution of the flax resistance genes and flax rust avirulence genes. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0602577103 – volume: 56 start-page: 169 year: 2008 ident: ref66 article-title: Systematic analysis of protein subcellular localization and interaction using high-throughput transient transformation of Arabidopsis seedlings. publication-title: Plant J doi: 10.1111/j.1365-313X.2008.03596.x – volume: 442 start-page: 39 year: 2006 ident: ref5 article-title: Intracellular pattern recognition receptors in the host response. publication-title: Nature doi: 10.1038/nature04946 – volume: 23 start-page: 454 year: 1998 ident: ref11 article-title: Plant disease-resistance proteins and the gene-for-gene concept. publication-title: Trends Biochem Sci doi: 10.1016/S0968-0004(98)01311-5 – volume: 24 start-page: 447 year: 1990 ident: ref50 article-title: Gene-for-gene complementarity in plant-pathogen interactions. publication-title: Annu Rev Genet doi: 10.1146/annurev.ge.24.120190.002311 – volume: 308 start-page: 1783 year: 2005 ident: ref15 article-title: Cladosporium Avr2 inhibits tomato Rcr3 protease required for Cf-2-dependent disease resistance. publication-title: Science doi: 10.1126/science.1111404 – volume: 20 start-page: 1169 year: 2008 ident: ref18 article-title: Fungal effector protein AVR2 targets diversifying defense-related cys proteases of tomato. publication-title: Plant Cell doi: 10.1105/tpc.107.056325 – volume: 11 start-page: 396 year: 2008 ident: ref19 article-title: Phytopathogen type III effector weaponry and their plant targets. publication-title: Curr Opin Plant Biol doi: 10.1016/j.pbi.2008.06.007 – volume: 1 start-page: 175 year: 2007 ident: ref34 article-title: A Pseudomonas syringae effector inactivates MAPKs to suppress PAMP-Induced immunity in plants. publication-title: Cell Host & Microbe doi: 10.1016/j.chom.2007.03.006 – volume: 22 start-page: 538 year: 2009 ident: ref67 article-title: Two type III secretion system effectors from Ralstonia solanacearum GMI1000 determine host-range specificity on tobacco. publication-title: Mol Plant Microbe Interact doi: 10.1094/MPMI-22-5-0538 – volume: 104 start-page: 2531 year: 2007 ident: ref16 article-title: Indirect activation of a plant nucleotide binding site-leucine-rich repeat protein by a bacterial protease. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0608779104 – volume: 9 start-page: 2700 year: 2007 ident: ref55 article-title: YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction. publication-title: Cell Microbiol doi: 10.1111/j.1462-5822.2007.00990.x – volume: 16 start-page: 2809 year: 2004 ident: ref31 article-title: A patch of surface-exposed residues mediates negative regulation of immune signaling by tomato Pto kinase. publication-title: Plant Cell doi: 10.1105/tpc.104.024141 – volume: 107 start-page: 815 year: 2001 ident: ref62 article-title: Why is p53 acetylated? publication-title: Cell doi: 10.1016/S0092-8674(01)00619-5 – volume: 13 start-page: 629 year: 2005 ident: ref63 article-title: Modulation of binding of DNA to the C-terminal domain of p53 by acetylation. publication-title: Structure doi: 10.1016/j.str.2005.01.020 – volume: 243 start-page: 6361 year: 1968 ident: ref58 article-title: Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones. publication-title: J Biol Chem – volume: 20 start-page: 1915 year: 2008 ident: ref65 article-title: XopD SUMO protease affects host transcription, promotes pathogen growth, and delays symptom development in xanthomonas-infected tomato leaves. publication-title: Plant Cell doi: 10.1105/tpc.108.058529 – volume: 121 start-page: 749 year: 2005 ident: ref17 article-title: Two Pseudomonas syringae type III effectors inhibit RIN4-regulated basal defense in Arabidopsis. publication-title: Cell doi: 10.1016/j.cell.2005.03.025 – volume: 99 start-page: 2404 year: 2002 ident: ref38 article-title: Resistance to Ralstonia solanacearum in Arabidopsis thaliana is conferred by the recessive RRS1-R gene, a member of a novel family of resistance genes. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.032485099 – volume: 61 start-page: 31 year: 2006 ident: ref52 article-title: Direct interaction between the tobacco mosaic virus helicase domain and the ATP-bound resistance protein, N factor during the hypersensitive response in tobacco plants. publication-title: Plant Mol Biol doi: 10.1007/s11103-005-5817-8 – volume: 13 start-page: 251 year: 2004 ident: ref64 article-title: Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. publication-title: Mol Cell doi: 10.1016/S1097-2765(03)00528-8 – volume: 108 start-page: 743 year: 2002 ident: ref13 article-title: RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. publication-title: Cell doi: 10.1016/S0092-8674(02)00661-X – volume: 29 start-page: 65 year: 1991 ident: ref35 article-title: Biology and epidemiology of bacterial wilt caused by pseudomonas solanacearum. publication-title: Annu Rev Phytopathol doi: 10.1146/annurev.py.29.090191.000433 – volume: 49 start-page: 1537 year: 2003 ident: ref54 article-title: Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease. publication-title: Mol Microbiol doi: 10.1046/j.1365-2958.2003.03666.x – volume: 268 start-page: 305 year: 1993 ident: ref60 article-title: Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 “tail” to DNA. publication-title: J Biol Chem doi: 10.1016/S0021-9258(18)54150-8 – volume: 34 start-page: D270 year: 2006 ident: ref41 article-title: MEROPS: the peptidase database. publication-title: Nucleic Acids Res doi: 10.1093/nar/gkj089 – volume: 60 start-page: 379 year: 2009 ident: ref2 article-title: A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors. publication-title: Annu Rev Plant Biol doi: 10.1146/annurev.arplant.57.032905.105346 – volume: 411 start-page: 826 year: 2001 ident: ref12 article-title: Plant pathogens and integrated defence responses to infection. publication-title: Nature doi: 10.1038/35081161 – volume: 18 start-page: 74 year: 2008 ident: ref29 article-title: Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases. publication-title: Curr Biol doi: 10.1016/j.cub.2007.12.020 – volume: 274 start-page: 2063 year: 1996 ident: ref7 article-title: Molecular Basis of Gene-for-Gene Specificity in Bacterial Speck Disease of Tomato. publication-title: Science doi: 10.1126/science.274.5295.2063 – volume: 444 start-page: 323 year: 2006 ident: ref1 article-title: The plant immune system. publication-title: Nature doi: 10.1038/nature05286 – volume: 449 start-page: 243 year: 2007 ident: ref30 article-title: The structural basis for activation of plant immunity by bacterial effector protein AvrPto. publication-title: Nature doi: 10.1038/nature06109 – volume: 112 start-page: 379 year: 2003 ident: ref14 article-title: Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance. publication-title: Cell doi: 10.1016/S0092-8674(03)00040-0 – volume: 318 start-page: 645 year: 2007 ident: ref26 article-title: Plant pathogen recognition mediated by promoter activation of the pepper Bs3 resistance gene. publication-title: Science doi: 10.1126/science.1144958 – volume: 53 start-page: 115 year: 2004 ident: ref48 article-title: Inventory and functional analysis of the large Hrp regulon in Ralstonia solanacearum: identification of novel effector proteins translocated to plant host cells through the type III secretion system. publication-title: Mol Microbiol doi: 10.1111/j.1365-2958.2004.04118.x – volume: 435 start-page: 1122 year: 2005 ident: ref27 article-title: R gene expression induced by a type-III effector triggers disease resistance in rice. publication-title: Nature doi: 10.1038/nature03630 – volume: 50 start-page: 377 year: 2003 ident: ref39 article-title: Xanthomonas type III effector XopD targets SUMO-conjugated proteins in planta. publication-title: Mol Microbiol doi: 10.1046/j.1365-2958.2003.03730.x – volume: 43 start-page: 873 year: 2005 ident: ref57 article-title: A single amino acid insertion in the WRKY domain of the Arabidopsis TIR-NBS-LRR-WRKY-type disease resistance protein SLH1 (sensitive to low humidity 1) causes activation of defense responses and hypersensitive cell death. publication-title: Plant J doi: 10.1111/j.1365-313X.2005.02500.x – volume: 7 start-page: 601 year: 2006 ident: ref22 article-title: Bacterial elicitation and evasion of plant innate immunity. publication-title: Nat Rev Mol Cell Biol doi: 10.1038/nrm1984 – volume: 280 start-page: 41537 year: 2005 ident: ref56 article-title: p300 modulates ATF4 stability and transcriptional activity independently of its acetyltransferase domain. publication-title: J Biol Chem doi: 10.1074/jbc.M505294200 – volume: 124 start-page: 803 year: 2006 ident: ref4 article-title: Host-microbe interactions: shaping the evolution of the plant immune response. publication-title: Cell doi: 10.1016/j.cell.2006.02.008 – volume: 112 start-page: 369 year: 2003 ident: ref21 article-title: Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the avrRpt2-directed elimination of RIN4. publication-title: Cell doi: 10.1016/S0092-8674(03)00036-9 – volume: 324 start-page: 742 year: 2009 ident: ref6 article-title: Innate immunity in plants: an arms race between pattern recognition receptors in plants and effectors in microbial pathogens. publication-title: Science doi: 10.1126/science.1171647 – volume: 318 start-page: 648 year: 2007 ident: ref25 article-title: A bacterial effector acts as a plant transcription factor and induces a cell size regulator. publication-title: Science doi: 10.1126/science.1144956 – volume: 20 start-page: 1017 year: 2009 ident: ref3 article-title: In the trenches of plant pathogen recognition: Role of NB-LRR proteins. publication-title: Semin Cell Dev Biol doi: 10.1016/j.semcdb.2009.04.010 – volume: 49 start-page: 389 year: 2003 ident: ref32 article-title: A translocated protein tyrosine phosphatase of Pseudomonas syringae pv. tomato DC3000 modulates plant defence response to infection. publication-title: Mol Microbiol doi: 10.1046/j.1365-2958.2003.03616.x – volume: 100 start-page: 8024 year: 2003 ident: ref9 article-title: Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1230660100 – volume: 9 start-page: 275 year: 1971 ident: ref49 article-title: Annu Rev Phytopathol – volume: 102 start-page: 6496 year: 2005 ident: ref53 article-title: The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally acylated target, RIN4, from Arabidopsis membranes to block RPM1 activation. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0500792102 – volume: 301 start-page: 1230 year: 2003 ident: ref20 article-title: Cleavage of Arabidopsis PBS1 by a bacterial type III effector. publication-title: Science doi: 10.1126/science.1085671 – volume: 10 start-page: 366 year: 2007 ident: ref36 article-title: Networks of WRKY transcription factors in defense signaling. publication-title: Curr Opin Plant Biol doi: 10.1016/j.pbi.2007.04.020 – volume: 7 start-page: 384 year: 2004 ident: ref40 article-title: Cysteine proteases in phytopathogenic bacteria: identification of plant targets and activation of innate immunity. publication-title: Curr Opin Plant Biol doi: 10.1016/j.pbi.2004.05.003 – volume: 11 start-page: 659 year: 1998 ident: ref37 article-title: Genetic characterization of RRS1, a recessive locus in Arabidopsis thaliana that confers resistance to the bacterial soilborne pathogen Ralstonia solanacearum. publication-title: Mol Plant Microbe Interact doi: 10.1094/MPMI.1998.11.7.659 – volume: 17 start-page: 633 year: 2004 ident: ref42 article-title: Characterization of the Xanthomonas AvrXv4 effector, a SUMO protease translocated into plant cells. publication-title: Mol Plant Microbe Interact doi: 10.1094/MPMI.2004.17.6.633 – volume: 103 start-page: 18574 year: 2006 ident: ref43 article-title: Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0608995103 – year: 2010 ident: ref10 article-title: Activation of an Arabidopsis Resistance Protein Is Specified by the in Planta Association of Its Leucine-Rich Repeat Domain with the Cognate Oomycete Effector. publication-title: Plant Cell – volume: 32 start-page: 210 year: 2007 ident: ref45 article-title: A newly discovered post-translational modification—the acetylation of serine and threonine residues. publication-title: Trends Biochem Sci doi: 10.1016/j.tibs.2007.03.007 – volume: 447 start-page: 284 year: 2007 ident: ref28 article-title: A type III effector ADP-ribosylates RNA-binding proteins and quells plant immunity. publication-title: Nature doi: 10.1038/nature05737 – volume: 9 start-page: 148 year: 1999 ident: ref59 article-title: Chromatin-modifying and -remodeling complexes. publication-title: Curr Opin Genet Dev doi: 10.1016/S0959-437X(99)80022-7 – reference: 35235614 - PLoS Pathog. 2022 Mar 2;18(3):e1010368 |
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| SubjectTerms | Acetylation Amino Acid Sequence Arabidopsis Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis - microbiology Arabidopsis Proteins - genetics Arabidopsis Proteins - immunology Arabidopsis Proteins - metabolism Arabidopsis thaliana Bacterial Proteins - genetics Bacterial Proteins - immunology Bacterial Proteins - metabolism Binding sites Blotting, Western Cell Nucleus - immunology Cell Nucleus - metabolism Cysteine Cysteine Endopeptidases - genetics Cysteine Endopeptidases - immunology Cysteine Endopeptidases - metabolism Enzymes Fluorescence Gene Expression Regulation, Plant Immune response Immunity, Innate - immunology Lysine - genetics Lysine - immunology Lysine - metabolism Microbiology/Plant-Biotic Interactions Molecular Sequence Data Molecular weight Mutation - genetics Physiological aspects Plant Biology/Plant-Biotic Interactions Plant Diseases - genetics Plant Diseases - immunology Plant Diseases - microbiology Plant Immunity Plant resistance Proteins Ralstonia solanacearum Ralstonia solanacearum - genetics Ralstonia solanacearum - metabolism Ralstonia solanacearum - pathogenicity Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - genetics Sequence Homology, Amino Acid Software |
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| Title | Autoacetylation of the Ralstonia solanacearum Effector PopP2 Targets a Lysine Residue Essential for RRS1-R-Mediated Immunity in Arabidopsis |
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