Phosphorylation of the conserved C-terminal domain of ribosomal P-proteins impairs the mode of interaction with plant toxins

FEBS Letters

article

Patrycja Horbowicz-Drożdżal¹  Karol Kamel²  Sebastian Kmiecik³  Lidia Borkiewicz⁴  Nilgun E. Tumer⁵  Pang-Chui Shaw⁶  Marek Tchórzewski¹  Przemysław Grela¹ 

[1] Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University;Institute of Bioorganic Chemistry, Polish Academy of Sciences;Biological and Chemical Research Centre, Faculty of Chemistry, University of Warsaw;Department of Biochemistry and Molecular Biology, Medical University of Lublin;Department of Plant Biology and Pathology, School of Environmental and Biological Sciences, Rutgers University;School of Life Sciences, The Chinese University of Hong Kong

关键词: P1/P2 proteins;    phosphorylation;    ribosomal stalk;    ribosome-inactivating protein;    ricin A chain;    trichosanthin;   

DOI  :  10.1002/1873-3468.14170

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ribosome is subjected to post-translational modifications, including phosphorylation, that affect its biological activity. Among ribosomal elements, the P-proteins undergo phosphorylation within the C terminus, the element which interacts with trGTPases or ribosome-inactivating proteins (RIPs); however, the role of phosphorylation has never been elucidated. Here, we probed the function of phosphorylation on the interaction of P-proteins with RIPs using the ribosomal P1-P2 dimer. We determined the kinetic parameters of the interaction with the toxins using biolayer interferometry and microscale thermophoresis. The results present the first mechanistic insight into the function of P-protein phosphorylation, showing that introduction of a negative charge into the C terminus of P1-P2 proteins promotes α-helix formation and decreases the affinity of the P-proteins for the RIPs.

【 授权许可】

Unknown