Universität Heidelberg looks for Scientific coordinator at the GreenRobust location Heidelberg (f/m/d) in Heidelberg - apply now!

Leibniz Institute of Plant Biochemistry (Halle) offers a Postdoctoral position in Biology

Activities Webinars ”MechanoBioTalks – Mechanics, Materials and Living Matter” is a webinar series supported by the GreenTE consortium and organized […]

AI-powered pipeline converts antibodies into functional intrabodies, enabling live-cell imaging of peptides and histone marks.

Abstract. Protein structure-based comparison provides a framework for uncovering deep evolutionary relationships that can escape conventional sequence-base

Generalist pathogens pose a challenge to plant immunity by infecting diverse hosts while harboring extensive intraspecific genetic variation. Whether evolutionary distant plant lineages rely on a shar...

An exciting opportunity has arisen for a Postdoctoral Researcher to join the Faulkner Group at the John Innes Centre, working on cutting-edge science in the field of Cell & Developmental Biology.

The power of hydrogen (pH) regulates virtually all cellular activities. In both plants and animals, cell-to-cell variations in pH correlate with key developmental transitions1–5, yet the underlying regulators and associated functions remain elusive. Here, we report that members of the REMORIN (REM) protein family function as inhibitors of the H+-ATPases thereby promoting extracellular pH (pHe) alkalinization. This, in turn, regulates various cell surface processes, including steroid hormone signaling, and coordinates developmental transitions in the Arabidopsis thaliana root. Inhibition of H+-ATPases by REMs represents an evolutionary innovation that predates the origin of the root system itself. This study thus uncovers an ancient alkalinization mechanism co-opted by the root developmental program and infers that pHe patterning may have shaped morphogenesis evolution.

Nucleotide-binding leucine-rich repeat (NLR) immune receptors sense pathogen molecules and oligomerize, initiating defense signaling. Some NLRs function poorly at elevated temperatures for unknown reasons. We show that temperature-sensitive NLRs retain ligand binding at elevated temperatures but are impaired in oligomerization. We identify key residues involved in temperature resilience. Structural modeling reveals stabilizing intramolecular interactions of the NB-ARC domain with surface residues of the adjacent leucine-rich repeat (LRR) that preserve receptor integrity and functionality under heat stress. These insights enable in silico classification of NLRs as temperature-sensitive or -tolerant and underpin design of temperature tolerant variants of temperature sensitive NLRs. These findings provide a mechanistic basis for temperature sensitivity in plant immune receptors and enable engineering of temperature-tolerant disease resistance in crops.