Description

• Title:
  Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors
• Creator:
  Filipek, Kamil;
  Blanchet, Sandra;
  Molestak, Eliza;
  Zaciura, Monika;
  Chih-Chien Wu, Colin;
  Horbowicz-Drożdżal, Patrycja;
  Grela, Przemysław;
  Zalewski, Mateusz;
  Kmiecik, Sebastian;
  González-Ibarra, Alan;
  Krokowski, Dawid;
  Latoch, Przemysław;
  Starosta, Agata L;
  Mołoń, Mateusz;
  Shao, Yutian;
  Borkiewicz, Lidia;
  Michalec-Wawiórka, Barbara;
  Wawiórka, Leszek;
  Kubiński, Konrad;
  Socała, Katarzyna;
  Wlaź, Piotr;
  Cunningham, Kyle W;
  Green, Rachel;
  Rodnina, Marina V;
  Tchórzewski, Marek
• Description:
  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.
• Object availability:
  free access
• Date:
  2024
• Type:
  Article;
  PeerReviewed
• Language:
  English
• Format:
  application/pdf
• Relation: http://eprints.ibb.waw.pl/2467 ;https://doi.org/10.1038/s44319-024-00297-1
• Subject:
  Q Science (General)
• Identifier: http://eprints.ibb.waw.pl/2467/1/filipek-et-al-2024-phosphorylation-of-p-stalk-proteins-defines-the-ribosomal-state-for-interaction-with-auxiliary.pdf ;
  Filipek, Kamil and Blanchet, Sandra and Molestak, Eliza and Zaciura, Monika and Chih-Chien Wu, Colin and Horbowicz-Drożdżal, Patrycja and Grela, Przemysław and Zalewski, Mateusz and Kmiecik, Sebastian and González-Ibarra, Alan and Krokowski, Dawid and Latoch, Przemysław and Starosta, Agata L and Mołoń, Mateusz and Shao, Yutian and Borkiewicz, Lidia and Michalec-Wawiórka, Barbara and Wawiórka, Leszek and Kubiński, Konrad and Socała, Katarzyna and Wlaź, Piotr and Cunningham, Kyle W and Green, Rachel and Rodnina, Marina V and Tchórzewski, Marek (2024) Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors. EMBO Reports .
• Data provider:
  Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk
• Can I use it?:
  seek permission
• Type:
  other