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Article: The structural basis for activation of plant immunity by bacterial effector protein AvrPto

TitleThe structural basis for activation of plant immunity by bacterial effector protein AvrPto
Authors
Issue Date2007
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/nature
Citation
Nature, 2007, v. 449 n. 7159, p. 243-247 How to Cite?
AbstractPathogenic microbes use effectors to enhance susceptibility in host plants. However, plants have evolved a sophisticated immune system to detect these effectors using cognate disease resistance proteins, a recognition that is highly specific, often elicits rapid and localized cell death, known as a hypersensitive response, and thus potentially limits pathogen growth. Despite numerous genetic and biochemical studies on the interactions between pathogen effector proteins and plant resistance proteins, the structural bases for such interactions remain elusive. The direct interaction between the tomato protein kinase Pto and the Pseudomonas syringae effector protein AvrPto is known to trigger disease resistance and programmed cell death through the nucleotide-binding site/leucine-rich repeat (NBS-LRR) class of disease resistance protein Prf. Here we present the crystal structure of an AvrPto-Pto complex. Contrary to the widely held hypothesis that AvrPto activates Pto kinase activity, our structural and biochemical analyses demonstrated that AvrPto is an inhibitor of Pto kinase in vitro. The AvrPto-Pto interaction is mediated by the phosphorylation-stabilized P+1 loop and a second loop in Pto, both of which negatively regulate the Prf-mediated defences in the absence of AvrPto in tomato plants. Together, our results show that AvrPto derepresses host defences by interacting with the two defence-inhibition loops of Pto. ©2007 Nature Publishing Group.
Persistent Identifierhttp://hdl.handle.net/10722/91918
ISSN
2015 Impact Factor: 38.138
2015 SCImago Journal Rankings: 21.936
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXing, Wen_HK
dc.contributor.authorZou, Yen_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorLiu, Jen_HK
dc.contributor.authorLuo, Xen_HK
dc.contributor.authorHuang, Qen_HK
dc.contributor.authorChen, Sen_HK
dc.contributor.authorZhu, Len_HK
dc.contributor.authorBi, Ren_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorWu, JWen_HK
dc.contributor.authorZhou, JMen_HK
dc.contributor.authorChai, Jen_HK
dc.date.accessioned2010-09-17T10:30:30Z-
dc.date.available2010-09-17T10:30:30Z-
dc.date.issued2007en_HK
dc.identifier.citationNature, 2007, v. 449 n. 7159, p. 243-247en_HK
dc.identifier.issn0028-0836en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91918-
dc.description.abstractPathogenic microbes use effectors to enhance susceptibility in host plants. However, plants have evolved a sophisticated immune system to detect these effectors using cognate disease resistance proteins, a recognition that is highly specific, often elicits rapid and localized cell death, known as a hypersensitive response, and thus potentially limits pathogen growth. Despite numerous genetic and biochemical studies on the interactions between pathogen effector proteins and plant resistance proteins, the structural bases for such interactions remain elusive. The direct interaction between the tomato protein kinase Pto and the Pseudomonas syringae effector protein AvrPto is known to trigger disease resistance and programmed cell death through the nucleotide-binding site/leucine-rich repeat (NBS-LRR) class of disease resistance protein Prf. Here we present the crystal structure of an AvrPto-Pto complex. Contrary to the widely held hypothesis that AvrPto activates Pto kinase activity, our structural and biochemical analyses demonstrated that AvrPto is an inhibitor of Pto kinase in vitro. The AvrPto-Pto interaction is mediated by the phosphorylation-stabilized P+1 loop and a second loop in Pto, both of which negatively regulate the Prf-mediated defences in the absence of AvrPto in tomato plants. Together, our results show that AvrPto derepresses host defences by interacting with the two defence-inhibition loops of Pto. ©2007 Nature Publishing Group.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/natureen_HK
dc.relation.ispartofNatureen_HK
dc.titleThe structural basis for activation of plant immunity by bacterial effector protein AvrPtoen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/nature06109en_HK
dc.identifier.pmid17694048-
dc.identifier.scopuseid_2-s2.0-34548606963en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34548606963&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume449en_HK
dc.identifier.issue7159en_HK
dc.identifier.spage243en_HK
dc.identifier.epage247en_HK
dc.identifier.isiWOS:000249394500055-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridXing, W=7102932876en_HK
dc.identifier.scopusauthoridZou, Y=36467252800en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridLiu, J=35080816100en_HK
dc.identifier.scopusauthoridLuo, X=35080765200en_HK
dc.identifier.scopusauthoridHuang, Q=7403634448en_HK
dc.identifier.scopusauthoridChen, S=35489933000en_HK
dc.identifier.scopusauthoridZhu, L=35378651100en_HK
dc.identifier.scopusauthoridBi, R=34973751500en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridWu, JW=7409250712en_HK
dc.identifier.scopusauthoridZhou, JM=12808066700en_HK
dc.identifier.scopusauthoridChai, J=7202678942en_HK
dc.identifier.citeulike1557870-

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