Multiple functional self-association interfaces in plant TIR domains.
The self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains has been implicated in signaling in plant and animal immunity receptors. Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 fromArabidopsisHere we show that the crystal structure of the TIR domain from theArabidopsisNLR suppressor of npr1-1, constitutive 1 (SNC1) contains both an L6-like interface involving helices αD and αE (DE interface) and an RPS4-like interface involving helices αA and αE (AE interface). Mutations in either the AE- or DE-interface region disrupt cell-death signaling activity of SNC1, L6, and RPS4 TIR domains and full-length L6 and RPS4. Self-association of L6 and RPS4 TIR domains is affected by mutations in either region, whereas only AE-interface mutations affect SNC1 TIR-domain self-association. We further show two similar interfaces in the crystal structure of the TIR domain from theArabidopsisNLR recognition ofPeronospora parasitica1 (RPP1). These data demonstrate that both the AE and DE self-association interfaces are simultaneously required for self-association and cell-death signaling in diverse plant NLRs.
School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia.|Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australia.
Xiaoxiao
X
Zhang
Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australia; stask@berkeley.edu maud.bernoux@csiro.au simon.williams@anu.edu.au peter.dodds@csiro.au b.kobe@uq.edu.au.
Maud
M
Bernoux
School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia.|School of Biological Sciences, Faculty of Science and Engineering, Flinders University, Adelaide, SA 5001, Australia.
Adam R
AR
Bentham
Department of Life Sciences, and School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang, Gyeongbuk 790-784, Republic of Korea.|Bioprotection Research Centre, Institute of Agriculture and Environment, Massey University, Palmerston North 4442, New Zealand.
Toby E
TE
Newman
School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia.|Institute for Glycomics, Griffith University, Southport, QLD 4222, Australia.
Thomas
T
Ve
School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia.
Lachlan W
LW
Casey
Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australia.|Department of Biology, Plant-Microbe Interactions, Utrecht University, 3584 CH Utrecht, The Netherlands.
Tom M
0000-0003-1056-7177
TM
Raaymakers
Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australia.|College of Biological Sciences, China Agricultural University, Beijing 100094, People's Republic of China.
Jian
J
Hu
School of Biomedical Sciences, Queensland University of Technology, Brisbane, QLD 4001, Australia.
Tristan I
TI
Croll
Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720.
Karl J
KJ
Schreiber
Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720; stask@berkeley.edu maud.bernoux@csiro.au simon.williams@anu.edu.au peter.dodds@csiro.au b.kobe@uq.edu.au.
Brian J
BJ
Staskawicz
School of Biological Sciences, Faculty of Science and Engineering, Flinders University, Adelaide, SA 5001, Australia.
Peter A
PA
Anderson
Department of Life Sciences, and School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang, Gyeongbuk 790-784, Republic of Korea.|Bioprotection Research Centre, Institute of Agriculture and Environment, Massey University, Palmerston North 4442, New Zealand.
Kee Hoon
KH
Sohn
School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia; stask@berkeley.edu maud.bernoux@csiro.au simon.williams@anu.edu.au peter.dodds@csiro.au b.kobe@uq.edu.au.|Research School of Biology, College of Medicine, Biology, and Environment, Australian National University, Canberra, ACT 0200, Australia.
Simon J
SJ
Williams
Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australia; stask@berkeley.edu maud.bernoux@csiro.au simon.williams@anu.edu.au peter.dodds@csiro.au b.kobe@uq.edu.au.
Peter N
PN
Dodds
School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia; stask@berkeley.edu maud.bernoux@csiro.au simon.williams@anu.edu.au peter.dodds@csiro.au b.kobe@uq.edu.au.
Bostjan
0000-0001-9413-9166
B
Kobe
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics* / Q000276:immunology / Q000382:microbiology; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D001665:Binding Sites; D016923:Cell Death / Q000235:genetics / Q000276:immunology; D019597:Flax / Q000235:genetics / Q000276:immunology / Q000382:microbiology; D018506:Gene Expression Regulation, Plant; D054884:Host-Pathogen Interactions; D008958:Models, Molecular; D009154:Mutation; D044742:Peronospora / Q000472:pathogenicity / Q000502:physiology; D010935:Plant Diseases / Q000235:genetics* / Q000276:immunology / Q000382:microbiology; D057865:Plant Immunity / Q000235:genetics; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D014026:Nicotiana / Q000235:genetics / Q000276:immunology / Q000382:microbiology
D029681:Arabidopsis Proteins; C095731:L6 protein, Linum usitatissimum; C105496:NPR1 protein, Arabidopsis; D010940:Plant Proteins; D011994:Recombinant Proteins; C482739:SNC1 protein, Arabidopsis; C097421:rps4 protein, plant
NLR; TIR domain; plant disease resistance; plant immunity; signaling by cooperative assembly formation