Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors.
Autor: | Filipek K; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Blanchet S; Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.; Institute for Integrative Biology of the Cell, I2BC, CEA, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France., Molestak E; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Zaciura M; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Wu CC; Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA.; Section of Translational Control of Gene Expression, RNA Biology Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA., Horbowicz-Drożdżal P; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Grela P; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Zalewski M; Biological and Chemical Research Center, Faculty of Chemistry, University of Warsaw, Warsaw, Poland., Kmiecik S; Biological and Chemical Research Center, Faculty of Chemistry, University of Warsaw, Warsaw, Poland., González-Ibarra A; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Krokowski D; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Latoch P; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland., Starosta AL; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland., Mołoń M; Institute of Biology, University of Rzeszow, Rzeszow, Poland., Shao Y; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Borkiewicz L; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland.; Department of Biochemistry and Molecular Biology, Medical University of Lublin, Aleje Racławickie 1, 20-059, Lublin, Poland., Michalec-Wawiórka B; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Wawiórka L; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Kubiński K; Department of Molecular Biology, Institute of Biological Sciences, John Paul II Catholic University of Lublin, Lublin, Poland., Socała K; Department of Animal Physiology and Pharmacology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Wlaź P; Department of Animal Physiology and Pharmacology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland., Cunningham KW; Department of Biology, Johns Hopkins University, Baltimore, MD, USA. kwc@jhu.edu., Green R; Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA. ragreen@jhmi.edu., Rodnina MV; Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. rodnina@mpinat.mpg.de., Tchórzewski M; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland. marek.tchorzewski@mail.umcs.pl. |
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Jazyk: | angličtina |
Zdroj: | EMBO reports [EMBO Rep] 2024 Oct 28. Date of Electronic Publication: 2024 Oct 28. |
DOI: | 10.1038/s44319-024-00297-1 |
Abstrakt: | Ribosomal action is facilitated by the orchestrated work of trans-acting factors and ribosomal elements, which are subject to regulatory events, often involving phosphorylation. One such element is the ribosomal P-stalk, which plays a dual function: it activates translational GTPases, which support basic ribosomal functions, and interacts with the Gcn2 kinase, linking the ribosomes to the ISR pathway. We show that P-stalk proteins, which form a pentamer, exist in the cell exclusively in a phosphorylated state at five C-terminal domains (CTDs), ensuring optimal translation (speed and accuracy) and may play a role in the timely regulation of the Gcn2-dependent stress response. Phosphorylation of the CTD induces a structural transition from a collapsed to a coil-like structure, and the CTD gains conformational freedom, allowing specific but transient binding to various protein partners, optimizing the ribosome action. The report reveals a unique feature of the P-stalk proteins, indicating that, unlike most ribosomal proteins, which are regulated by phosphorylation in an on/off manner, the P-stalk proteins exist in a constantly phosphorylated state, which optimizes their interaction with auxiliary factors. (© 2024. The Author(s).) |
Databáze: | MEDLINE |
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