Unveiling the Ro60-Ro52 complex
DOI:
https://doi.org/10.17179/excli2024-7141Keywords:
Ro52/Trim21, Ro60/Trove2, transient complex, QCM-D, PLA, IIFAbstract
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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Copyright (c) 2024 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
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