Laura R Rodríguez, Jesus Vicente de Julián-Ortiz, Fernando Rubio de la Rúa, Augusto Juste-Dolz, Ángel Maquieira, Haydar A Mohammad-Salim, Sofiane Benmetir, Federico V Pallardó, Pilar González-Cabo, David Gimenez-Romero
{"title":"揭开 Ro60-Ro52 建筑群的神秘面纱。","authors":"Laura R Rodríguez, Jesus Vicente de Julián-Ortiz, Fernando Rubio de la Rúa, Augusto Juste-Dolz, Ángel Maquieira, Haydar A Mohammad-Salim, Sofiane Benmetir, Federico V Pallardó, Pilar González-Cabo, David Gimenez-Romero","doi":"10.17179/excli2024-7141","DOIUrl":null,"url":null,"abstract":"<p><p>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<sub>a</sub> ≈ (3.7 ± 0.3) x 10<sup>6</sup> M<sup>-1</sup>, 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. See also the graphical abstract(Fig. 1).</p>","PeriodicalId":12247,"journal":{"name":"EXCLI Journal","volume":"23 ","pages":"888-903"},"PeriodicalIF":3.8000,"publicationDate":"2024-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11231564/pdf/","citationCount":"0","resultStr":"{\"title\":\"Unveiling the Ro60-Ro52 complex.\",\"authors\":\"Laura R Rodríguez, Jesus Vicente de Julián-Ortiz, Fernando Rubio de la Rúa, Augusto Juste-Dolz, Ángel Maquieira, Haydar A Mohammad-Salim, Sofiane Benmetir, Federico V Pallardó, Pilar González-Cabo, David Gimenez-Romero\",\"doi\":\"10.17179/excli2024-7141\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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<sub>a</sub> ≈ (3.7 ± 0.3) x 10<sup>6</sup> M<sup>-1</sup>, 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. See also the graphical abstract(Fig. 1).</p>\",\"PeriodicalId\":12247,\"journal\":{\"name\":\"EXCLI Journal\",\"volume\":\"23 \",\"pages\":\"888-903\"},\"PeriodicalIF\":3.8000,\"publicationDate\":\"2024-06-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11231564/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"EXCLI Journal\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.17179/excli2024-7141\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/1/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"Q1\",\"JCRName\":\"BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"EXCLI Journal","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.17179/excli2024-7141","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/1/1 0:00:00","PubModel":"eCollection","JCR":"Q1","JCRName":"BIOLOGY","Score":null,"Total":0}
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. See also the graphical abstract(Fig. 1).
期刊介绍：
EXCLI Journal publishes original research reports, authoritative reviews and case reports of experimental and clinical sciences.
The journal is particularly keen to keep a broad view of science and technology, and therefore welcomes papers which bridge disciplines and may not suit the narrow specialism of other journals. Although the general emphasis is on biological sciences, studies from the following fields are explicitly encouraged (alphabetical order):
aging research, behavioral sciences, biochemistry, cell biology, chemistry including analytical chemistry, clinical and preclinical studies, drug development, environmental health, ergonomics, forensic medicine, genetics, hepatology and gastroenterology, immunology, neurosciences, occupational medicine, oncology and cancer research, pharmacology, proteomics, psychiatric research, psychology, systems biology, toxicology
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