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Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors

  1. Author:
    Filipek, Kamil [ORCID]
    Blanchet, Sandra [ORCID]
    Molestak, Eliza
    Zaciura, Monika
    Wu,Colin
    Horbowicz-Drozdzal, Patrycja
    Grela, Przemyslaw [ORCID]
    Zalewski, Mateusz [ORCID]
    Kmiecik, Sebastian
    González-Ibarra, Alan
    Krokowski, Dawid
    Latoch, Przemyslaw [ORCID]
    Starosta, Agata L [ORCID]
    Molon, Mateusz [ORCID]
    Shao, Yutian [ORCID]
    Borkiewicz, Lidia [ORCID]
    Michalec-Wawiórka, Barbara
    Wawiórka, Leszek
    Kubinski, Konrad [ORCID]
    Socala, Katarzyna [ORCID]
    Wlaz, Piotr [ORCID]
    Cunningham, Kyle W [ORCID]
    Green, Rachel [ORCID]
    Rodnina, Marina V [ORCID]
    Tchórzewski, Marek [ORCID]

  2. Author Address

    1Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Sklodowska University, Lublin, Poland. 2Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. 3Institute for Integrative Biology of the Cell, I2BC, CEA, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France. 4Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA. 5Section of Translational Control of Gene Expression, RNA Biology Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA. 6Biological and Chemical Research Center, Faculty of Chemistry, University of Warsaw, Warsaw, Poland. 7Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland. 8Institute of Biology, University of Rzeszow, Rzeszow, Poland. 9Department of Biochemistry and Molecular Biology, Medical University of Lublin, Aleje Raclawickie 1, 20-059, Lublin, Poland. 10Department of Molecular Biology, Institute of Biological Sciences, John Paul II Catholic University of Lublin, Lublin, Poland. 11Department of Animal Physiology and Pharmacology, Institute of Biological Sciences, Maria Curie-Sklodowska University, Lublin, Poland. 12Department of Biology, Johns Hopkins University, Baltimore, MD, USA. kwc@jhu.edu. 13Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA. ragreen@jhmi.edu. 14Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. rodnina@mpinat.mpg.de. 15Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Sklodowska University, Lublin, Poland. marek.tchorzewski@mail.umcs.pl.
    1. Year: 2024
    2. Date: Oct 28
    3. Epub Date: 2024 10 28
  2. Journal: EMBO Reports
  4. Type of Article: Article
  1. Abstract:

    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).

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  2. DOI: 10.1038/s44319-024-00297-1
  3. PMID: 39468350
  4. PII : 10.1038/s44319-024-00297-1

Library Notes

  1. Fiscal Year: FY2024-2025
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