Poster
Magdalena Krzymowska
Institute of Biochemistry and Biophysics, Polish Academy of Sciences
Warsaw, POLAND
Marta Grech-Baran
PhD
Institute of Biochemistry and Biophysics, Polish Academy of Sciences
Warsaw, POLAND
Marek Zurczak
Institute of Biochemistry and Biophysics, Polish Academy of Sciences
Warsaw, Mazowieckie, Poland
Malgorzata Lichocka
Institute of Biochemistry and Biophysics, Polish Academy of Sciences
Warsaw, Mazowieckie, Poland
Recognition of pathogen effectors by plant NLR receptors initiates a defense response that often culminates in cell death, referred to as the hypersensitive response (HR). While several mechanisms have been identified to prevent the mis-activation of these receptors, how the immediate downstream signaling is controlled remains unclear.
Resistance to Tobacco Mosaic Virus (TMV) is mediated by N, a tobacco TNL receptor, and NRG1, a CNL-type helper protein. The binding of p50, the helicase fragment of the TMV replicase, leads to oligomerization of N. Consequently, NRG1 assembly into oligomers that function as calcium channels.
It was previously reported that the N gene undergoes alternative splicing and that the truncated form of N (NL) is blocking HR development.
Our findings suggest that although NL is able to bind p50, in contrast to the full-length N receptor (Ns), it cannot oligomerize upon p50 recognition nor activate NRG1. Blue Native PAGE analyses revealed that NL interferes with the formation of Ns resistosomes, offering a potential mechanism for HR suppression and terminating downstream signalling.