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Intrinsically disordered proteins SAID1/2 condensate on SERRATE for dual inhibition of miRNA biogenesis in Arabidopsis
Intrinsically disordered proteins (IDPs) SAID1/2 are hypothetic dentin sialophosphoprotein-like proteins, but their true functions are unknown. Here, we identified SAID1/2 as negative regulators of SERRATE (SE), a core factor in miRNA biogenesis complex (microprocessor). Loss-of-function double muta...
Autores principales: | , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10083546/ https://www.ncbi.nlm.nih.gov/pubmed/36972460 http://dx.doi.org/10.1073/pnas.2216006120 |
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author | Shang, Baoshuan Wang, Lin Yan, Xingxing Li, Yanjun Li, Changhao Wu, Chaohua Wang, Tian Guo, Xiang Choi, Suk Won Zhang, Tianru Wang, Ziying Tong, Chun-Yip Oh, Taerin Zhang, Xiao Wang, Zhiye Peng, Xu Zhang, Xiuren |
author_facet | Shang, Baoshuan Wang, Lin Yan, Xingxing Li, Yanjun Li, Changhao Wu, Chaohua Wang, Tian Guo, Xiang Choi, Suk Won Zhang, Tianru Wang, Ziying Tong, Chun-Yip Oh, Taerin Zhang, Xiao Wang, Zhiye Peng, Xu Zhang, Xiuren |
author_sort | Shang, Baoshuan |
collection | PubMed |
description | Intrinsically disordered proteins (IDPs) SAID1/2 are hypothetic dentin sialophosphoprotein-like proteins, but their true functions are unknown. Here, we identified SAID1/2 as negative regulators of SERRATE (SE), a core factor in miRNA biogenesis complex (microprocessor). Loss-of-function double mutants of said1; said2 caused pleiotropic developmental defects and thousands of differentially expressed genes that partially overlapped with those in se. said1; said2 also displayed increased assembly of microprocessor and elevated accumulation of microRNAs (miRNAs). Mechanistically, SAID1/2 promote pre-mRNA processing 4 kinase A-mediated phosphorylation of SE, causing its degradation in vivo. Unexpectedly, SAID1/2 have strong binding affinity to hairpin-structured pri-miRNAs and can sequester them from SE. Moreover, SAID1/2 directly inhibit pri-miRNA processing by microprocessor in vitro. Whereas SAID1/2 did not impact SE subcellular compartmentation, the proteins themselves exhibited liquid–liquid phase condensation that is nucleated on SE. Thus, we propose that SAID1/2 reduce miRNA production through hijacking pri-miRNAs to prevent microprocessor activity while promoting SE phosphorylation and its destabilization in Arabidopsis. |
format | Online Article Text |
id | pubmed-10083546 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-100835462023-09-27 Intrinsically disordered proteins SAID1/2 condensate on SERRATE for dual inhibition of miRNA biogenesis in Arabidopsis Shang, Baoshuan Wang, Lin Yan, Xingxing Li, Yanjun Li, Changhao Wu, Chaohua Wang, Tian Guo, Xiang Choi, Suk Won Zhang, Tianru Wang, Ziying Tong, Chun-Yip Oh, Taerin Zhang, Xiao Wang, Zhiye Peng, Xu Zhang, Xiuren Proc Natl Acad Sci U S A Biological Sciences Intrinsically disordered proteins (IDPs) SAID1/2 are hypothetic dentin sialophosphoprotein-like proteins, but their true functions are unknown. Here, we identified SAID1/2 as negative regulators of SERRATE (SE), a core factor in miRNA biogenesis complex (microprocessor). Loss-of-function double mutants of said1; said2 caused pleiotropic developmental defects and thousands of differentially expressed genes that partially overlapped with those in se. said1; said2 also displayed increased assembly of microprocessor and elevated accumulation of microRNAs (miRNAs). Mechanistically, SAID1/2 promote pre-mRNA processing 4 kinase A-mediated phosphorylation of SE, causing its degradation in vivo. Unexpectedly, SAID1/2 have strong binding affinity to hairpin-structured pri-miRNAs and can sequester them from SE. Moreover, SAID1/2 directly inhibit pri-miRNA processing by microprocessor in vitro. Whereas SAID1/2 did not impact SE subcellular compartmentation, the proteins themselves exhibited liquid–liquid phase condensation that is nucleated on SE. Thus, we propose that SAID1/2 reduce miRNA production through hijacking pri-miRNAs to prevent microprocessor activity while promoting SE phosphorylation and its destabilization in Arabidopsis. National Academy of Sciences 2023-03-27 2023-04-04 /pmc/articles/PMC10083546/ /pubmed/36972460 http://dx.doi.org/10.1073/pnas.2216006120 Text en Copyright © 2023 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/This article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Biological Sciences Shang, Baoshuan Wang, Lin Yan, Xingxing Li, Yanjun Li, Changhao Wu, Chaohua Wang, Tian Guo, Xiang Choi, Suk Won Zhang, Tianru Wang, Ziying Tong, Chun-Yip Oh, Taerin Zhang, Xiao Wang, Zhiye Peng, Xu Zhang, Xiuren Intrinsically disordered proteins SAID1/2 condensate on SERRATE for dual inhibition of miRNA biogenesis in Arabidopsis |
title | Intrinsically disordered proteins SAID1/2 condensate on SERRATE for dual inhibition of miRNA biogenesis in Arabidopsis |
title_full | Intrinsically disordered proteins SAID1/2 condensate on SERRATE for dual inhibition of miRNA biogenesis in Arabidopsis |
title_fullStr | Intrinsically disordered proteins SAID1/2 condensate on SERRATE for dual inhibition of miRNA biogenesis in Arabidopsis |
title_full_unstemmed | Intrinsically disordered proteins SAID1/2 condensate on SERRATE for dual inhibition of miRNA biogenesis in Arabidopsis |
title_short | Intrinsically disordered proteins SAID1/2 condensate on SERRATE for dual inhibition of miRNA biogenesis in Arabidopsis |
title_sort | intrinsically disordered proteins said1/2 condensate on serrate for dual inhibition of mirna biogenesis in arabidopsis |
topic | Biological Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10083546/ https://www.ncbi.nlm.nih.gov/pubmed/36972460 http://dx.doi.org/10.1073/pnas.2216006120 |
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