Marek Tchórzewski earned his Master of Science degree in Biology, with a focus on Microbiology, from Maria Curie-Skłodowska University in Lublin, Poland. He then pursued his PhD in biochemistry and molecular biology at Kyoto University in Japan (Promoter of the PhD thesis, Prof. Kenji Soda). Following his doctoral studies, Marek Tchórzewski undertook postdoctoral research at the University of Southern Denmark in Odense (under supervision of Prof. Olaf-Georg Issinger), where he worked in the field of cell biology, specifically exploring posttranslational modifications of proteins via phosphorylation by CK2 protein kinase. Marek Tchórzewski also completed additional postdoctoral work at Lund University in Sweden (under the supervision of Prof. Ander Liljas), where his research concentrated on the structure and function of ribosomal particles. His work focused particularly on the role of the GTPase-associated center and ribosomal P proteins.

Early in his research career, Marek Tchórzewski joined the Department of Molecular Biology at Maria Curie-Skłodowska University in Lublin, initially serving as an assistant professor before being promoted to an associate professor. Currently, he holds a full professorship at the same institution and serves as the head of the Department of Molecular Biology. In addition to his academic responsibilities, Marek Tchórzewski founded the Intravital Cell Imaging Laboratory, which is part of a larger Polish collaborative infrastructure project known as the National Multidisciplinary Laboratory of Functional Nanomaterials (NanoFun). He was involved in the establishment of research units, including the Protein Bioengineering Laboratory, which specializes in protein‒protein interaction analyses and incorporates cutting-edge native-MS technology (currently under direct supervision of Dr. P. Grela). Marek Tchórzewski was also a cofounder of the newly established Metabolomic Laboratory (under direct supervision of Dr. D. Krokowski), a collaborative endeavor between the Institute of Biological Sciences and the ECOTECH-COMPLEX Analytical and Programme Centre for Advanced Environmentally Friendly Technologies, located at Maria Curie-Skłodowska University in Lublin.

Research projects have focused on the regulation of gene expression at the translational level, with the ribosome serving as the primary research target. Specifically, the role of ribosomal proteins in the performance of the translational machinery is examined, with an emphasis on the decoding of genetic information during the elongation phase of translation. This work explored the reciprocal interactions between ribosomes and protein factors known as translational GTPases (trGTPases). The trGTPases function as molecular switches, cycling between an active GTP-bound form and an inactive GDP-bound form, conferring a unidirectional trajectory for the translational apparatus at the expense of GTP hydrolysis. The landing platform for trGTPases on the ribosome is the GTPase Associated Center (GAC), which is located on the large ribosomal subunit. GAC plays a critical role in activating trGTPases. A substantial part of the GAC is made up of a set of ribosomal proteins called P-stalk proteins, which are responsible for recruiting trGTPases and stimulating factor-dependent GTP hydrolysis. This project aims to unravel the structure and function of these GAC elements, with a particular focus on P-stalk proteins, in relation to the regulation of translational machinery in both steady-state and pathological conditions, such as cancer development.

Additionally, research has focused on the molecular mechanisms of Ribosome Inactivating Proteins (RIPs). The objective of this study is to understand the interactions between these toxins and the ribosome, particularly how P-stalk—an element critical for ribosomal translation factor recruitment—is highly affected by toxins to inhibit translation.

In the course of these projects, ribosomal heterogeneity has been explored, as has the role of ribosomal protein isoforms and posttranslational modifications such as phosphorylation. The main aims are to shed light on the phenomenon of specialized ribosomes and to reveal how the translational machinery fine-tunes ribosome responses to external and internal environmental fluctuations, especially in the context of cancer development.

Selected publications

Kulczyk A.W., Sorzano C.O.S., Grela P, Tchórzewski M., Tumer N.E., Li X.P. Cryo-EM structure of Shiga toxin 2 in complex with the native ribosomal P-stalk reveals residues involved in the binding interaction. Journal of Biological Chemistry, (2023), 299(1):102795.

Filipek K., Deryło K., Michalec-Wawiórka B., Zaciura M., González-Ibarra A., Krokowski D., Latoch P., Starosta A.L., Czapiński J., Rivero-Müller A., Wawiórka L., Tchórzewski M. Identification of a novel alternatively spliced isoform of the ribosomal uL10 protein. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, (2023) 1866(1):194890.

Shao Y., Molestak E., Su W., Stankevič M., Tchórzewski M. Sordarin - An anti-fungal antibiotic with a unique modus operandi. British Journal of Pharmacology, (2022) 179(6), 1125–1145.

Szajwaj M., Wawiórka L., Molestak E., Michalec-Wawiórka B., Mołoń M., Wojda I., Tchórzewski M. The influence of ricin-mediated rRNA depurination on the translational machinery in vivo - New insight into ricin toxicity. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, (2019), 1866(12):118554.

Grela P., Szajwaj M., Horbowicz-Drożdżal P., Tchórzewski M. How Ricin Damages the Ribosome. Toxins (Basel). (2019), 11(5). pii: E241.

Deryło K., Michalec-Wawiórka B., Krokowski D., Wawiórka L., Hatzoglou M., Tchórzewski M. The uL10 protein, a component of the ribosomal P-stalk, is released from the ribosome in nucleolar stress. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, (2018), 1865(1):34-47.

Wawiórka L., Molestak E., Szajwaj M., Michalec-Wawiórka B., Mołoń M., Borkiewicz L., Grela P., Boguszewska A., Tchórzewski M. Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation. Molecular and Cellular Biology, (2017) 37(17):e00060-17.

Grela P., Li X.P., Horbowicz P., Dźwierzyńska M., Tchórzewski M., Tumer N.E. Human ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus. Scientific Reports, (2017) 7(1):5608.

Wawiórka L., Krokowski D., Gordiyenko Y., Krowarsch D., Robinson C.V., Adam I., Grankowski N., Tchórzewski M. In vivo formation of Plasmodium falciparum ribosomal stalk - A unique mode of assembly without stable heterodimeric intermediates. Biochimica et Biophysica Acta (BBA) - General Subjects, (2015) 1850(1), 150-158.

Ban N., Beckmann R., Cate J.H., Dinman J.D., Dragon F., Ellis S.R., Lafontaine D.L., Lindahl L., Liljas A., Lipton J.M., McAlear M.A., Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V., Spahn C.M., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J., Williamson J.R., Wilson D., Yonath A., Yusupov M. A new system for naming ribosomal proteins. Current Opinion in Structural Biology, (2014) 24, 165-169.