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Molecular BiologyBMC Biology
Peer-reviewed journal article

CDE-1 suppresses the production of risiRNA by coupling polyuridylation and degradation of 26S rRNA

Yun WangiD, Chenchun WengiD, Xiangyang CheniD, Xufei ZhouiD, Xinya HuangiD, Meng-qiu Dong, Chengming ZhuiD, Shouhong GuangiD

PDFDOIPreprint

Abstract

Antisense ribosomal siRNAs (risiRNAs) 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). There are three polyuridylation polymerases, CDE-1, PUP-2, and PUP-3, in C. elegans. Here, we found that CDE-1 is specifically involved in suppressing risiRNA production. CDE-1 localizes to perinuclear granules in the germline and uridylates both Argonaute-associated 22G-RNAs and 26S rRNAs at the 3-ends. Immunoprecipitation followed by mass spectrometry (IP-MS) revealed that CDE-1 interacts with SUSI-1(ceDIS3L2). Consistent with those results, both CDE-1 and SUSI-1(ceDIS3L2) are required for the inheritance of RNAi. Therefore, this work identified a rRNA surveillance machinery of rRNAs that couples terminal polyuridylation and degradation.

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