Plant NLR proteins enable the immune systemto recognize and respond to pathogen attack.An early consequence of immune activation is transcriptional reprogramming.SomeNLRs have been shownto act in the nucleus and inter...Plant NLR proteins enable the immune systemto recognize and respond to pathogen attack.An early consequence of immune activation is transcriptional reprogramming.SomeNLRs have been shownto act in the nucleus and interact with transcription factors.The Rx1 NLR protein of potato binds and distorts doublestranded DNA.However,the components of the chromatin-localized Rx1 complex are largely unknown.Here,we report a physical and functional interaction between Rx1 and NbDBCP,a bromodomaincontaining chromatin-interacting protein.NbDBCP accumulates in the nucleoplasmand nucleolus,interacts with chromatin,and redistributes Rx1 tothe nucleolus in a subpopulation of imaged cells.Rx1 overexpression reduces the interaction between NbDBCP and chromatin.NbDBCP is a negative regulator of Rx1-mediated immune responses to potato virus X(PVX),and this activity requires an intact bromodomain.Previously,Rx1 has been shown to regulate the DNA-binding activity of a Golden2-like transcription factor,NbGlk1.Rx1 and NbDBCP act synergistically to reduce NbGlk1 DNA binding,suggesting a mode of action for NbDBCP’s inhibitory effect on immunity.This study provides new mechanistic insight into the mechanism by which a chromatin-localized NLR complex co-ordinates immune signaling after pathogen perception.展开更多
基金supported by Biotechnology and Biological Sciences Research Council grant BB/M007405/1(to M.J.C.and L.-O.P.)the Dutch Technology Foundation STW and Earth and Life Sciences ALW(to E.J.S.,O.C.A.S.,and A.G.)VICI project no.865.14.003(to F.L.W.T.)(Netherlands Organization for Scientific Research).
文摘Plant NLR proteins enable the immune systemto recognize and respond to pathogen attack.An early consequence of immune activation is transcriptional reprogramming.SomeNLRs have been shownto act in the nucleus and interact with transcription factors.The Rx1 NLR protein of potato binds and distorts doublestranded DNA.However,the components of the chromatin-localized Rx1 complex are largely unknown.Here,we report a physical and functional interaction between Rx1 and NbDBCP,a bromodomaincontaining chromatin-interacting protein.NbDBCP accumulates in the nucleoplasmand nucleolus,interacts with chromatin,and redistributes Rx1 tothe nucleolus in a subpopulation of imaged cells.Rx1 overexpression reduces the interaction between NbDBCP and chromatin.NbDBCP is a negative regulator of Rx1-mediated immune responses to potato virus X(PVX),and this activity requires an intact bromodomain.Previously,Rx1 has been shown to regulate the DNA-binding activity of a Golden2-like transcription factor,NbGlk1.Rx1 and NbDBCP act synergistically to reduce NbGlk1 DNA binding,suggesting a mode of action for NbDBCP’s inhibitory effect on immunity.This study provides new mechanistic insight into the mechanism by which a chromatin-localized NLR complex co-ordinates immune signaling after pathogen perception.
