UNVEILING THE RO60-RO52 COMPLEX

October 11, 2024

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Publicated to:Excli Journal. 23 888-903 - 2024-01-01 23(), DOI: 10.17179/excli2024-7141

Authors: Rodriguez, Laura R; de Julian-Ortiz, Jesus Vicente; de la Rua, Fernando Rubio; Juste-Dolz, Augusto; Maquieira, Angel; Mohammad-Salim, Haydar A; Benmetir, Sofiane; Pallardo, Federico, V; Gonzalez-Cabo, Pilar; Gimenez-Romero, David

Affiliations

CIBER Rare Dis CIBERER - Author

Lund Univ, Fac Med, Lund Stem Cell Ctr, Stem Cells Aging & Neurodegenerat Grp,Dept Expt Me - Author

Univ Politecn Valencia, Ctr Res & Innovat Bioengn Ci2B, Camino Vera S-N - Author

Univ Sci & Technol Oran Mohamed BOUDIAF, Fac Chem, Proc & Environm Engn Lab LIPE, POB 1503, El Mnaouer 31000 - Author

Univ Valencia, Fac Chem, Dept Phys Chem, C-Doctor Moliner 50 - Author

Univ Valencia, Fac Pharm, Dept Phys Chem, Mol Topol & Drug Design Res Unit, Av Vicent Andres Estelles S-N - Author

Univ Valencia, Univ Politecn Valencia, Inst Interuniv Invest Reconocimiento Mol & Desarro, Camino Vera S-N - Author

Univ Zakho, Fac Sci, Dept Chem, Duhok 42001 - Author

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 K a approximate to (3.7 +/- 0.3) x 10 6 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 Ro60YRNA 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.

Keywords

DiagramsIifImmunityMolprobityPlaProtein-protein dockingQcm-dRibonucleoproteinsRo 60-kda autoantigenRo52/trim21Ro60/trove2Structure validationTransient complex

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Bibliometric impact. Analysis of the contribution and dissemination channel

The work has been published in the journal Excli Journal due to its progression and the good impact it has achieved in recent years, according to the agency WoS (JCR), it has become a reference in its field. In the year of publication of the work, 2024 there are still no calculated indicators, but in 2023, it was in position 10/107, thus managing to position itself as a Q1 (Primer Cuartil), in the category Biology. Notably, the journal is positioned above the 90th percentile.

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This work has been carried out with international collaboration, specifically with researchers from: Algeria; Iraq; Sweden.

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