Novel insights into the assembly of the yeast translation initiation multifactor complex: The critical role of <scp>eIF5</scp>
into the peptidyl (P) site of the 40S ribosomal subunit. While some interactions between eIFs have been described in the context of the PIC, the interactions within the MFC remain poorly understood. Here, we combine biophysical and biochemical approaches, including mass photometry and native mass spectrometry, with structural biology methods such as electron microscopy, to gain deeper insights into the MFC architecture. Our findings provide novel insights into the critical role of eIF5 during MFC assembly. Notably, two copies of eIF5 are involved in the formation of the MFC. We propose that one eIF5 molecule engages eIF2β and eIF2γ, whereas a second eIF5 molecule interacts with eIF1 together with eIF3c.
Authors
- J.L. Llacer (ORCID: https://orcid.org/0000-0001-5304-1795)
- Carolina Espinosa (ORCID: https://orcid.org/0009-0005-7504-3835)
- José Rafael Ciges‐Tomas
- Borja Sáez de la Fuente
- Marisa López‐Redondo
- Laura Villamayor‐Belinchón
Institutions
- Centre National de la Recherche Scientifique (FR)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Novo Nordisk Foundation (DK)
- CEA Grenoble (FR)
- Instituto de Biomedicina de Valencia (ES)
- Institut de Biologie Structurale (FR)
- Instituto de Investigación de Enfermedades Raras (ES)
- Université Grenoble Alpes (FR)
Publication Details
- Journal
- Protein Science
- Published
- 2026-04-07
- DOI
- https://doi.org/10.1002/pro.70550
- Primary Topic
- RNA and protein synthesis mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Agence Nationale de la Recherche
- Generalitat Valenciana
- Novo Nordisk
- Centre National de la Recherche Scientifique
- French Infrastructure for Integrated Structural Biology