摘要详情

ID / 提交时间

453 / 2019-02-26 08:29:37

标题

TIR Domains of Plant Immune Receptors are NAD+ Consuming Enzymes that Promote Cell Death

关键字

TIR, NADase, Cell Death, Immunity

主题及专题

全体主题 > Plant Microbe Interactions & Microbiomes

状态

摘要录用

作者

Li Wan / Department of Biology and Howard Hughes Medical Institute, University of North Carolina, Chapel Hill, NC 27599

Kow Essuman / Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110

Ryan Anderson / Department of Biology and Howard Hughes Medical Institute, University of North Carolina, Chapel Hill, NC 27599

Yo Sasaki / Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110

Freddy Monteiro / Center for Research in Agricultural Genomics (CRAG), CSIC-IRTA-UAB-UB, 08193 Barcelona

Eui-Hwan Chung / Department of Biology and Howard Hughes Medical Institute, University of North Carolina, Chapel Hill, NC 27599

Erin Osborne Nishimura / Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523

Aaron DiAntonio / Department of Developmental Biology, Washington University School of Medicine, St. Louis, MO 63110

Jeffrey Milbrandt / Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110

Jeffery Dangl / Department of Biology and Howard Hughes Medical Institute, University of North Carolina, Chapel Hill, NC 27599

Marc Nishimura / Department of Biology, Colorado State University, Fort Collins, CO 80523

摘要

Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors activate cell death and confer resistance to pathogens. The mechanism by which plant NLRs trigger cell death remains obscure. We demonstrate that plant TIR (Toll/interleukin-1 receptor) domains are enzymes capable of degrading NAD+. Both cell death induction and NADase activity of plant ‘TIR-only’ proteins and TIR domains derived from TIR-NBS-LRR (TNL) immune receptors require known self-association interfaces and a putative catalytic glutamic acid conserved in both bacterial TIR NADases and the mammalian SARM1 TIR NADase. We identify a variant form of cADPR as an in vitro TIR-dependent NAD+ breakdown product and an in planta biomarker of TIR enzymatic activity. We show that TIR enzymatic activity is induced by pathogen recognition, and functions upstream of EDS1 and NRG1, two proteins required for TIR immune function. Thus, plant TIR-NLR receptors require a conserved enzymatic function to transduce recognition of pathogens into a cell death response.