TIR domain-associated nucleotides with functions in plant immunity and beyond.

Natsumi Maruta, Mitchell Sorbello, Bryan Y J Lim, Helen Y McGuinness, Yun Shi, Thomas Ve, Bostjan Kobe

Journal: Current opinion in plant biology 2023;73():102364

PMID: 37086529

Full Text on Elsevier Science View on PubMed

Abstract

TIR (Toll/interlukin-1 receptor) domains are found in archaea, bacteria and eukaryotes, featured in proteins generally associated with immune functions. In plants, they are found in a large group of NLRs (nucleotide-binding leucine-rich repeat receptors), NLR-like proteins and TIR-only proteins. They are also present in effector proteins from phytopathogenic bacteria that are associated with suppression of host immunity. TIR domains from plants and bacteria are enzymes that cleave NAD (nicotinamide adenine dinucleotide, oxidized form) and other nucleotides. In dicot plants, TIR-derived signalling molecules activate downstream immune signalling proteins, the EDS1 (enhanced disease susceptibility 1) family proteins, and in turn helper NLRs. Recent work has brought major advances in understanding how TIR domains work, how they produce signalling molecules and how these products signal.

Address: The University of Queensland, School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, Brisbane, QLD 4072, Australia.; Institute for Glycomics, Griffith University, Southport, QLD 4222, Australia.; The University of Queensland, School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, Brisbane, QLD 4072, Australia. Electronic address: [email protected].

DOI: 10.1016/j.pbi.2023.102364

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MeSH Terms: Nucleotides, Plant Immunity, Plants, Protein Domains, NLR Proteins, Bacteria, Plant Diseases