Unveiling the Ro60-Ro52 complex

  1. Laura R. Rodríguez 7
  2. Jesus Vicente de Julián-Ortiz 4
  3. Fernando Rubio de la Rúa 2
  4. Augusto Juste-Dolz 5
  5. Ángel Maquieira 8
  6. Haydar Abdulhakim Mohammad-Salim 3
  7. Sofiane Benmetir 9
  8. Federico Vicente Pallardó 6
  9. Pilar González-Cabo 1
  10. David Gimenez-Romero 10
  1. 1 Department of Physiology, Faculty of Medicine and Dentistry. University of Valencia-INCLIVA, 46010 Valencia, Spain. E-mail: Pilar.Gonzalez-Cabo@uv.es
  2. 2 Department of Physical Chemistry, Faculty of Chemistry, University of Valencia, C/ Doctor Moliner 50, 46100, Burjassot, Spain
  3. 3 Molecular Topology and Drug Design Research Unit, Department of Physical Chemistry, Faculty of Pharmacy, University of Valencia, Av. Vicent Andrés Estellés s/n, 46100 Valencia, Spain; Faculty of Science, Department of Chemistry, University of Zakho, Zakho, Duhok 42001, Kurdistan Region, Iraq
  4. 4 Molecular Topology and Drug Design Research Unit, Department of Physical Chemistry, Faculty of Pharmacy, University of Valencia, Av. Vicent Andrés Estellés s/n, 46100 Valencia, Spain
  5. 5 Center for Research and Innovation on Bioengineering (Ci2B), Universitat Politècnica de València, Camino de Vera s/n, 46022 Valencia, Spain
  6. 6 Department of Physiology, Faculty of Medicine and Dentistry. University of Valencia-INCLIVA, 46010 Valencia, Spain; CIBER Rare Diseases (CIBERER), 46010 Valencia, Spain
  7. 7 Present address: Stem Cells, Aging and Neurodegeneration Group, Department of Experimental Medical Science, Faculty of Medicine, Lund Stem Cell Center, Lund University, 22184, Lund, Sweden
  8. 8 Departamento de Química, Polytechnic University of Valencia, Camino de Vera s/n 46022, Valencia, Spain; Instituto Interuniversitario de Investigación de Reconocimiento Molecular y Desarrollo Tecnológico (IDM), Universitat Politècnica de València, Universitat de València, Camino de Vera s/n, 46022 Valencia, Spain
  9. 9 Molecular Topology and Drug Design Research Unit, Department of Physical Chemistry, Faculty of Pharmacy, University of Valencia, Av. Vicent Andrés Estellés s/n, 46100 Valencia, Spain; Process and Environmental Engineering Laboratory (LIPE), Faculty of Chemistry, University of Science and Technology of Oran Mohamed BOUDIAF, P.O. Box 1503, El Mnaouer, 31000 Oran, Algeria
  10. 10 Department of Physical Chemistry, Faculty of Chemistry, University of Valencia, C/ Doctor Moliner 50, 46100, Burjassot, Spain. E-mail: giroda@uv.es
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Journal:
EXCLI Journal

ISSN: 1611-2156

Year of publication: 2024

Volume: 23

Pages: 888-903

Type: Article

DOI: 10.17179/EXCLI2024-7141 GOOGLE SCHOLAR lock_openOpen access editor

More publications in: EXCLI Journal

Abstract

The coexistence within a subcellular complex of inter-cellular proteins Ro60, responsible for preserving ncRNA quality, and Ro52, involved in intracellular proteolysis, has been a subject of ongoing debate. Employing molecular docking in tandem with experimental methods like Quartz Crystal Microbalance with Dissipation (QCM-D), Proximity Ligation Assay (PLA), and Indirect Immunofluorescence (IIF), we reveal the presence of Ro60 associating with Ro52 within the cytoplasm. This result unveils the formation of a weak transient complex with a Ka ≈ (3.7 ± 0.3) x 106 M-1, where the toroid-shaped Ro60 structure interacts with the Ro52’s Fc receptor, aligning horizontally within the PRY-SPRY domains of the Ro52’s homodimer. The stability of this complex relies on the interaction between Ro52 chain A and specific Ro60 residues, such as K133, W177, or L185, vital in the Ro60-YRNA bond. These findings bridge the role of Ro60 in YRNA management with Ro52's function in intracellular proteolysis, emphasizing the potential impact of transient complexes on cellular pathways.