Identification of whole-cell dsRNA-binding proteins by phase separation

Interactions between double-stranded RNA (dsRNA) and proteins play an important role in cellular homeostasis by regulating the editing, stability, and splicing of intracellular RNA. The identification of dsRNA-binding proteins (dsRBPs) is key; however, it has long been challenging to purify dsRBPs f...

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Main Authors: Zhixiang Yang, Junwei Zhou, Zhuang Li, Jiahui Guo, Liurong Fang, Xun Xiao, Shaobo Xiao
Format: Article
Language:English
Published: Taylor & Francis Group 2024-12-01
Series:RNA Biology
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Online Access:https://www.tandfonline.com/doi/10.1080/15476286.2024.2386498
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author Zhixiang Yang
Junwei Zhou
Zhuang Li
Jiahui Guo
Liurong Fang
Xun Xiao
Shaobo Xiao
author_facet Zhixiang Yang
Junwei Zhou
Zhuang Li
Jiahui Guo
Liurong Fang
Xun Xiao
Shaobo Xiao
author_sort Zhixiang Yang
collection DOAJ
description Interactions between double-stranded RNA (dsRNA) and proteins play an important role in cellular homeostasis by regulating the editing, stability, and splicing of intracellular RNA. The identification of dsRNA-binding proteins (dsRBPs) is key; however, it has long been challenging to purify dsRBPs from cells. In this study, we developed a novel method, dsRBPC (dsRNA-binding protein capture), to purify cellular dsRBPs based on classic phase separation purification procedures. A global dsRNA-binding proteome of LLC-PK1 cells was obtained, and we identified 1326 dsRBPs, including 1303 putative novel dsRBPs. Functional analyses suggested that these enriched dsRBPs are mainly associated with rRNA processing, RNA splicing, transcriptional regulation, and nucleocytoplasmic transport. We also found that the ARM (armadillo/beta-catenin-like repeats) motif is a previously unknown dsRNA-binding domain, as demonstrated by biochemical experiments. Collectively, this study provides a useful approach for dsRBP identification and the discovery of a global dsRNA-binding proteome to comprehensively map the dsRNA – protein interaction network.
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id doaj-art-03c2f8681f7143a1abae7ee543f8e3b9
institution Kabale University
issn 1547-6286
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language English
publishDate 2024-12-01
publisher Taylor & Francis Group
record_format Article
series RNA Biology
spelling doaj-art-03c2f8681f7143a1abae7ee543f8e3b92024-12-11T07:47:43ZengTaylor & Francis GroupRNA Biology1547-62861555-85842024-12-0121182083310.1080/15476286.2024.2386498Identification of whole-cell dsRNA-binding proteins by phase separationZhixiang Yang0Junwei Zhou1Zhuang Li2Jiahui Guo3Liurong Fang4Xun Xiao5Shaobo Xiao6National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, ChinaNational Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, ChinaNational Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, ChinaNational Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, ChinaNational Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, ChinaNational Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, ChinaNational Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, ChinaInteractions between double-stranded RNA (dsRNA) and proteins play an important role in cellular homeostasis by regulating the editing, stability, and splicing of intracellular RNA. The identification of dsRNA-binding proteins (dsRBPs) is key; however, it has long been challenging to purify dsRBPs from cells. In this study, we developed a novel method, dsRBPC (dsRNA-binding protein capture), to purify cellular dsRBPs based on classic phase separation purification procedures. A global dsRNA-binding proteome of LLC-PK1 cells was obtained, and we identified 1326 dsRBPs, including 1303 putative novel dsRBPs. Functional analyses suggested that these enriched dsRBPs are mainly associated with rRNA processing, RNA splicing, transcriptional regulation, and nucleocytoplasmic transport. We also found that the ARM (armadillo/beta-catenin-like repeats) motif is a previously unknown dsRNA-binding domain, as demonstrated by biochemical experiments. Collectively, this study provides a useful approach for dsRBP identification and the discovery of a global dsRNA-binding proteome to comprehensively map the dsRNA – protein interaction network.https://www.tandfonline.com/doi/10.1080/15476286.2024.2386498dsRNA-binding proteinsdsRNA-binding protein capturedsRNA-binding proteomedsRNA-binding domainphase separation
spellingShingle Zhixiang Yang
Junwei Zhou
Zhuang Li
Jiahui Guo
Liurong Fang
Xun Xiao
Shaobo Xiao
Identification of whole-cell dsRNA-binding proteins by phase separation
RNA Biology
dsRNA-binding proteins
dsRNA-binding protein capture
dsRNA-binding proteome
dsRNA-binding domain
phase separation
title Identification of whole-cell dsRNA-binding proteins by phase separation
title_full Identification of whole-cell dsRNA-binding proteins by phase separation
title_fullStr Identification of whole-cell dsRNA-binding proteins by phase separation
title_full_unstemmed Identification of whole-cell dsRNA-binding proteins by phase separation
title_short Identification of whole-cell dsRNA-binding proteins by phase separation
title_sort identification of whole cell dsrna binding proteins by phase separation
topic dsRNA-binding proteins
dsRNA-binding protein capture
dsRNA-binding proteome
dsRNA-binding domain
phase separation
url https://www.tandfonline.com/doi/10.1080/15476286.2024.2386498
work_keys_str_mv AT zhixiangyang identificationofwholecelldsrnabindingproteinsbyphaseseparation
AT junweizhou identificationofwholecelldsrnabindingproteinsbyphaseseparation
AT zhuangli identificationofwholecelldsrnabindingproteinsbyphaseseparation
AT jiahuiguo identificationofwholecelldsrnabindingproteinsbyphaseseparation
AT liurongfang identificationofwholecelldsrnabindingproteinsbyphaseseparation
AT xunxiao identificationofwholecelldsrnabindingproteinsbyphaseseparation
AT shaoboxiao identificationofwholecelldsrnabindingproteinsbyphaseseparation