ILANIT 2023

Atlas of tandem kinase proteins across the plant kingdom

Tamara Reveguk 1,2 Andrii Fatiukha 1,2,3 Evgeniy Potapenko 1,2 Hanan Sela 1 Valentyna Klymiuk 1,2,3 Curtis Pozniak 3 Thomas Wicker 4 Gitta Coaker 5 Tzion Fahima 1,2
1Institute of Evolution, University of Haifa, Israel
2The Department of Evolutionary and Environmental Biology, University of Haifa, Israel
3Crop Development Centre and Department of Plant Sciences,, University of Saskatchewan, Canada
4Department of Plant and Microbial Biology, University of Zurich, Switzerland
5Department of Plant Pathology, University of California, USA

Plants are an essential part of worldwide food production. Unfortunately, crop production is downgraded by various biotic stresses. An urgent task is to generate a new breeding material resistant to multiple pathogens and pests.

Plant pathogens can modulate plant metabolism and immune responses to their benefit by secreting effector proteins into plant cells. In turn, plants have numerous intracellular nucleotide-binding leucine-rich repeat (NLRs) receptors that are powerful components of effector-triggered immunity. Most functionally characterized plant disease resistance genes encode NLRs specific to certain pathogen races, which rapidly evolving pathogens may overcome.

The discovery of the wheat stripe rust resistance gene Yr15 and barley stem rust resistance gene Rpg1 encoding a rather nontypical resistance protein with a combination of two kinase domains prompted a new chapter in plant immunology. To date, numerous tandem kinase proteins (TKPs) from cereal crops have been discovered. However, both their evolutionary history and mechanism of action remain poorly understood.

The creation of the TKPs’ Atlas shall play a pivotal role in the future discoveries of TKP evolution and molecular function. Defining TKPs as protein sequences with two or more protein kinase domains, we scanned the genomes of 105 plant species and discovered TKPs across all Plant kingdom. We found that over half of the discovered TPKs have kinase domains lacking critical catalytically important residues (thus, representing pseudokinases) likely serving as decoys for the effector recognition in TKP-related immune responses.