EXCLI Journal : Experimental and Clinical Sciences (Jun 2024)

Unveiling the Ro60-Ro52 complex

  • Laura R. Rodríguez,
  • Jesus Vicente de Julián-Ortiz,
  • Fernando Rubio de la Rúa,
  • Augusto Juste-Dolz,
  • Ángel Maquieira,
  • Haydar Abdulhakim Mohammad-Salim,
  • Sofiane Benmetir,
  • Federico Vicente Pallardó,
  • Pilar González-Cabo,
  • David Gimenez-Romero

DOI
https://doi.org/10.17179/excli2024-7141
Journal volume & issue
Vol. 23
pp. 888 – 903

Abstract

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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.

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