In this seminar, hosted by Jens Tilsner from our Cell and Molecular Sciences group, Dr Martin Cann (Durham University) will discuss the role of plant NLR (Nucleotide Binding and C-terminal Leucine Rich Repeat) -type receptors in immune-dependent chromatin remodelling.
Abstract
​Nucleotide Binding and C-terminal Leucine Rich Repeat (NLR) proteins are key immune regulators that enable plant cells to respond to pathogen attack. Several NLRs act in the nucleus, however, conserved nuclear targets that support their role in immunity are unknown. We observe a structural homology between the nucleotide-binding domain of the Rx1 NLR of potato and DNA replication origin-binding proteins. Consistent with this, Rx1 binds, bends, and melts DNA. Facets of this biochemistry are conserved among NLRs from monocot and dicot species indicating a mechanism generic to at least a subset of NLRs. The coat protein of potato virus X triggers Rx1-DNA binding that requires correct subcellular localization and cytoplasmic activation of Rx1. Rx1 further interacts with a core complex of a transcription factor, chromatin remodelling protein, and proteins that recognise histone epigenetic modifications. These data establish DNA distortion as central to Rx1 immune signalling and defines nuclear DNA as the first conserved molecular target of an activated plant NLR.
Biography
Dr Martin Cann researches in the general area of biochemistry with a specific interest in the mechanistic basis of signalling modulated by nucleotides. This interest carries across bacterial, animal, and plant systems.