CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNA
Abstract Background Modification of RNAs, particularly at the terminals, is critical for various essential cell processes; for example, uridylation is implicated in tumorigenesis, proliferation, stem cell maintenance, and immune defense against viruses and retrotransposons. Ribosomal RNAs can be reg...
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BMC
2020-09-01
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Online Access: | http://link.springer.com/article/10.1186/s12915-020-00850-z |
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author | Yun Wang Chenchun Weng Xiangyang Chen Xufei Zhou Xinya Huang Yonghong Yan Chengming Zhu |
author_facet | Yun Wang Chenchun Weng Xiangyang Chen Xufei Zhou Xinya Huang Yonghong Yan Chengming Zhu |
author_sort | Yun Wang |
collection | DOAJ |
description | Abstract Background Modification of RNAs, particularly at the terminals, is critical for various essential cell processes; for example, uridylation is implicated in tumorigenesis, proliferation, stem cell maintenance, and immune defense against viruses and retrotransposons. Ribosomal RNAs can be regulated by antisense ribosomal siRNAs (risiRNAs), which downregulate pre-rRNAs through the nuclear RNAi pathway in Caenorhabditis elegans. However, the biogenesis and regulation of risiRNAs remain obscure. Previously, we showed that 26S rRNAs are uridylated at the 3′-ends by an unknown terminal polyuridylation polymerase before the rRNAs are degraded by a 3′ to 5′ exoribonuclease SUSI-1(ceDIS3L2). Results Here, we found that CDE-1, one of the three C.elegans polyuridylation polymerases (PUPs), is specifically involved in suppressing risiRNA production. CDE-1 localizes to perinuclear granules in the germline and uridylates Argonaute-associated 22G-RNAs, 26S, and 5.8S rRNAs at the 3′-ends. Immunoprecipitation followed by mass spectrometry (IP-MS) revealed that CDE-1 interacts with SUSI-1(ceDIS3L2). Consistent with these results, both CDE-1 and SUSI-1(ceDIS3L2) are required for the inheritance of RNAi. Conclusions This work identified a rRNA surveillance machinery of rRNAs that couples terminal polyuridylation and degradation. |
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language | English |
last_indexed | 2024-12-21T13:02:21Z |
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spelling | doaj.art-045c4616636f4435a31e76ffd5872da52022-12-21T19:03:07ZengBMCBMC Biology1741-70072020-09-0118111310.1186/s12915-020-00850-zCDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNAYun Wang0Chenchun Weng1Xiangyang Chen2Xufei Zhou3Xinya Huang4Yonghong Yan5Chengming Zhu6National Science Center for Physical Sciences at Microscale Division of Molecular & Cell Biophysics, School of Life Sciences, University of Science and Technology of ChinaNational Science Center for Physical Sciences at Microscale Division of Molecular & Cell Biophysics, School of Life Sciences, University of Science and Technology of ChinaNational Science Center for Physical Sciences at Microscale Division of Molecular & Cell Biophysics, School of Life Sciences, University of Science and Technology of ChinaNational Science Center for Physical Sciences at Microscale Division of Molecular & Cell Biophysics, School of Life Sciences, University of Science and Technology of ChinaNational Science Center for Physical Sciences at Microscale Division of Molecular & Cell Biophysics, School of Life Sciences, University of Science and Technology of ChinaNational Institute of Biological SciencesNational Science Center for Physical Sciences at Microscale Division of Molecular & Cell Biophysics, School of Life Sciences, University of Science and Technology of ChinaAbstract Background Modification of RNAs, particularly at the terminals, is critical for various essential cell processes; for example, uridylation is implicated in tumorigenesis, proliferation, stem cell maintenance, and immune defense against viruses and retrotransposons. Ribosomal RNAs can be regulated by antisense ribosomal siRNAs (risiRNAs), which downregulate pre-rRNAs through the nuclear RNAi pathway in Caenorhabditis elegans. However, the biogenesis and regulation of risiRNAs remain obscure. Previously, we showed that 26S rRNAs are uridylated at the 3′-ends by an unknown terminal polyuridylation polymerase before the rRNAs are degraded by a 3′ to 5′ exoribonuclease SUSI-1(ceDIS3L2). Results Here, we found that CDE-1, one of the three C.elegans polyuridylation polymerases (PUPs), is specifically involved in suppressing risiRNA production. CDE-1 localizes to perinuclear granules in the germline and uridylates Argonaute-associated 22G-RNAs, 26S, and 5.8S rRNAs at the 3′-ends. Immunoprecipitation followed by mass spectrometry (IP-MS) revealed that CDE-1 interacts with SUSI-1(ceDIS3L2). Consistent with these results, both CDE-1 and SUSI-1(ceDIS3L2) are required for the inheritance of RNAi. Conclusions This work identified a rRNA surveillance machinery of rRNAs that couples terminal polyuridylation and degradation.http://link.springer.com/article/10.1186/s12915-020-00850-zrRNAsiRNAArgonauterisiRNACDE-1SUSI-1 |
spellingShingle | Yun Wang Chenchun Weng Xiangyang Chen Xufei Zhou Xinya Huang Yonghong Yan Chengming Zhu CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNA BMC Biology rRNA siRNA Argonaute risiRNA CDE-1 SUSI-1 |
title | CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNA |
title_full | CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNA |
title_fullStr | CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNA |
title_full_unstemmed | CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNA |
title_short | CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of rRNA |
title_sort | cde 1 suppresses the production of risirna by coupling polyuridylation and degradation of rrna |
topic | rRNA siRNA Argonaute risiRNA CDE-1 SUSI-1 |
url | http://link.springer.com/article/10.1186/s12915-020-00850-z |
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