Universität zu Köln 

Prof. Dr. Jane Parker

Max-Planck-Institut für Pflanzenzüchtungsforschung, Köln
email: parker@mpipz.mpg.de
phone: +49-(0)221 5062 303
website

PD Dr. Karsten Niefind

Institut für Biochemie, Universität zu Köln
email: Karsten.Niefind@uni-koeln.de
phone: 0221 470-6444?
website

In plants and animals, activation of innate immune responses by intracellular receptors involves dynamic changes in the subcellular localisations, assemblies and activities of signalling complexes. The Arabidopsis nucleo-cytoplasmic protein EDS1, together with its partners PAD4 and SAG101, coordinates receptor-triggered host cell reprogramming by a series of post-translational changes affecting EDS1 intracellular distribution and defence programming activity. Characterisation of the molecular configurations of different EDS1 complexes suggests that transitions between EDS1 homomeric dimers and EDS1-SAG101 or EDS1-PAD4 heterodimers are important for resistance signal relay. A crystal structure of an EDS1-SAG101 heterodimer which we recently solved offers a new approach to understanding the nature of post-translational changes determining EDS1 functions and associations. We will use the structural information to test importance of particular amino acids and domains for EDS1-SAG101 binding and relate these to immune signalling activities in the plant. We will adopt computational approaches to model small ligand-docking sites inferred from the structure and test these biochemically and functionally. We will also undertake crystallisation studies of further functional, stabilized or transition states of EDS1. The data should provide insights to how EDS1 complexes are modified by a pathogen stimulus to induce cellular reprogramming in defence.

Running time: 07/2011 – 06/2015

Recent publications:

Parker & Niefind

Wagner, S., Stuttmann, J., Rietz, S., Guerois, R., Brunstein, E., Bautor, J., Niefind, K., and Parker, J.E. (2014). Structural Basis for Signaling by Exclusive EDS1 Heteromeric Complexes with SAG101 or PAD4 in Plant Innate Immunity. Cell Host Microbe. 2013 Dec 11;14(6):619-30. Pubmed

Rietz, S., Stamm, A., Malonek, S., Wagner, S., Becker, D., Medina-Escobar, N., Vlot, A.C., Feys, B.J., Niefind, K., and Parker, J.E. (2011). Different roles of EDS1 bound to and dissociated from PAD4 in Arabidopsis immunity. New Phytol. 191, 107-19.

Wagner, S., Rietz, S., Parker, J.E., and Niefind, K. (2011). Crystallisation and preliminary crystallographic analysis of Arabidopsis thaliana EDS1, a key component of plant defense, in complex with its signaling partner SAG101. Acta Crystallogr. Section F. 67, 245-8.

Raaf, J., Bischoff, N., Klopffleisch, K., Brunstein, E., Olsen, B.B., Vilk, G., Litchfield, D.W., Issinger, O.G., and Niefind, K. (2011). Interaction between CK2? and CK2?, the subunits of protein kinase CK2: thermodynamic contributions of key residues on the CK2? surface. Biochemistry 50, 512-522.

Niefind

Raaf, J., Guerra, B., Neundorf, I., Bopp, B., Issinger, O.G., Jose, J., Pietsch, M., and Niefind, K. ( 2013). First structure of protein kinase CK2 catalytic subunit with an effective CK2?-competitive ligand. ACS Chem Biol. 8, 901-7. PubMed

Parker

Shin, J., Heidrich, K., Sanchez-Villarreal, A., Parker, J.E. and Davis, S.J. (2012). TIME FOR COFFEE represses MYC2 protein accumulation to provide time-of-day regulation of jasmonate signaling. Plant Cell 24, 2470-2482.

Stuttmann, J., Hubberten, H.-M., Rietz, S., Kaur, J., Muskett, P, Guerois, R., Bednarek, P., Hoefgen, R. and Parker, J.E. (2011). Perturbation of Arabidopsis amino acid metabolism casues incompatibility with the adapted biotrophic pathogen Hyaloperonospora arabidopsidis. Plant Cell 23, 2788-2803.

Garcia, A.V., Blanvillain-Baufumé, S., Huibers, R.P., Wiermer, M, Li, G., Gobbato, E., Rietz, S., and Parker, J.E. (2010). Balanced nuclear and cytoplasmic activities of EDS1 are required for a complete plant innate immune response. PLoS Path. 6, e1000970.

Straus, M.R., Rietz, S., ver Loren van Themat, E., Bartsch, M., and Parker, J.E. (2010). Salicylic acid antagonism of EDS1-driven cell death is important for Arabidopsis immune and oxidative stress responses. Plant J. 62, 628-640.

Cheng, Y.T, Wiermer, M., Germain, H., Bi, D., Xu, F., Garcia, A.V., Wirthmueller, L., Depres, C., Parker, J.E., Zhang, Y., and Li, X. (2009). Nuclear pore complex component MOS7/Nup88 is required for plant innate immunity and nuclear accumulation of defense regulators. Plant Cell 21, 2503-2516.

Mühlenbock, P., Szechy?ska-Hebda, M., P?aszczyca, M., Baudo, M., Mullineaux. P.M., Parker, J.E., Karpi?ska, B., and Karpi?ski, S. (2008). Chloroplast signaling and LESION SIMULATING DISEASE 1 regulate crosstalk between light acclimation and immunity in Arabidopsis. Plant Cell 20, 2339-2356.

Wirthmueller, L., Zhang, Y., Jones, J.D.G., and Parker, J.E. (2007). Nuclear accumulation of the Arabidopsis immune receptor RPS4 is necessary for triggering EDS1-dependent defence. Curr. Biol. 17, 2023-2029.

Bartsch, M., Gobbato, E., Bednarek, P., Debey, S., Schultze, J.L., Bautor, J., and Parker, J.E. (2006). Salicylic acid independent ENHANCED DISEASE SUSCEPTIBILITY1 signaling in Arabidopsis immunity and cell death is regulated by the monooxygenase FMO1 and the Nudix hydrolase NUDT7. Plant Cell 18, 1038-1051.

Brodersen, P., Petersen, M., Nielsen, H.B., Zhu, S., Newman, M.A., Shokat, K.M., Rietz, S., Parker, J.E., and Mundy, J. (2006). Arabidopsis MAP kinase 4 regulates salicylic acid- and jasmonic acid/ethylene-dependent responses via EDS1 and PAD4. Plant J. 47, 532-546.

Feys, B.J., Wiermer, M., Bhat, R.A., Moisan, L.J., Medina-Escobar, N., Neu, C., Cabral A., and Parker, J.E. (2005). Arabidopsis SENESCENCE ASSOCIATED GENE101 stabilizes and signals within an ENHANCED DISEASE SUSCEPTIBILITY1 complex in plant innate immunity. Plant Cell 17, 2601-2613.