NAD + cleavage activity by animal and plant TIR domains in cell death pathways.

Autor: Horsefield S; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Burdett H; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Zhang X; Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australia.; Plant Sciences Division, Research School of Biology, The Australian National University, Canberra ACT 2601, Australia., Manik MK; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Shi Y; Institute for Glycomics, Griffith University, Southport, QLD 4222, Australia., Chen J; Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australia.; Plant Sciences Division, Research School of Biology, The Australian National University, Canberra ACT 2601, Australia., Qi T; Department of Plant and Microbial Biology, University of California Berkeley, Berkeley, CA 94720, USA., Gilley J; John van Geest Centre for Brain Repair, Department of Clinical Neurosciences, University of Cambridge, ED Adrian Building, Forvie Site, Robinson Way, Cambridge CB2 0PY, UK.; Babraham Institute, Babraham, Cambridge CB22 3AT, UK., Lai JS; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Rank MX; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Casey LW; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.; Centre for Microscopy and Microanalysis, University of Queensland, Brisbane, QLD 4072, Australia., Gu W; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Ericsson DJ; Macromolecular Crystallography (MX) Beamlines, Australian Synchrotron, Melbourne, VIC 3168, Australia., Foley G; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Hughes RO; Disarm Therapeutics, 400 Technology Square, Cambridge, MA 02139, USA., Bosanac T; Disarm Therapeutics, 400 Technology Square, Cambridge, MA 02139, USA., von Itzstein M; Institute for Glycomics, Griffith University, Southport, QLD 4222, Australia., Rathjen JP; Plant Sciences Division, Research School of Biology, The Australian National University, Canberra ACT 2601, Australia., Nanson JD; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Boden M; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia., Dry IB; Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Urrbrae, SA 5064, Australia., Williams SJ; Plant Sciences Division, Research School of Biology, The Australian National University, Canberra ACT 2601, Australia., Staskawicz BJ; Department of Plant and Microbial Biology, University of California Berkeley, Berkeley, CA 94720, USA., Coleman MP; John van Geest Centre for Brain Repair, Department of Clinical Neurosciences, University of Cambridge, ED Adrian Building, Forvie Site, Robinson Way, Cambridge CB2 0PY, UK.; Babraham Institute, Babraham, Cambridge CB22 3AT, UK., Ve T; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia. b.kobe@uq.edu.au t.ve@griffith.edu.au peter.dodds@csiro.au.; Institute for Glycomics, Griffith University, Southport, QLD 4222, Australia., Dodds PN; Agriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australia. b.kobe@uq.edu.au t.ve@griffith.edu.au peter.dodds@csiro.au., Kobe B; School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia. b.kobe@uq.edu.au t.ve@griffith.edu.au peter.dodds@csiro.au.
Jazyk: angličtina
Zdroj: Science (New York, N.Y.) [Science] 2019 Aug 23; Vol. 365 (6455), pp. 793-799.
DOI: 10.1126/science.aax1911
Abstrakt: SARM1 (sterile alpha and TIR motif containing 1) is responsible for depletion of nicotinamide adenine dinucleotide in its oxidized form (NAD + ) during Wallerian degeneration associated with neuropathies. Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors recognize pathogen effector proteins and trigger localized cell death to restrict pathogen infection. Both processes depend on closely related Toll/interleukin-1 receptor (TIR) domains in these proteins, which, as we show, feature self-association-dependent NAD + cleavage activity associated with cell death signaling. We further show that SARM1 SAM (sterile alpha motif) domains form an octamer essential for axon degeneration that contributes to TIR domain enzymatic activity. The crystal structures of ribose and NADP + (the oxidized form of nicotinamide adenine dinucleotide phosphate) complexes of SARM1 and plant NLR RUN1 TIR domains, respectively, reveal a conserved substrate binding site. NAD + cleavage by TIR domains is therefore a conserved feature of animal and plant cell death signaling pathways.
(Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.)
Databáze: MEDLINE
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