Journal
ELIFE
Volume 10, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.62449
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Funding
- Ministry of Science and Technology, Taiwan [103-2311-B-009 -003-MY2, 105-2311-B-009 -002-MY3]
- National Institutes of Health [2R01DC005991, R01 DC015758]
- National Chiao Tung University The higher education sprout project of the National Chiao Tung University
- National Chiao Tung University The higher education sprout project of the Ministry of Education, Taiwan
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The Caenorhabditis elegans expresses two distinct proteins, MUT-7 and CeWRN-1, which contribute differently to small interfering RNA synthesis and neuronal plasticity. The collaboration of exonuclease and helicase domains in these proteins may promote RNA loading into a heterochromatin complex, thereby affecting olfactory plasticity in the worm.
Caenorhabditis elegans expresses human Werner syndrome protein (WRN)orthologs as two distinct proteins: MUT-7, with a 30' -50' exonuclease domain, and CeWRN-1, with helicase domains. How these domains cooperate remains unclear. Here, we demonstrate the different contributions of MUT-7 and CeWRN-1 to 22G small interfering RNA (siRNA) synthesis and the plasticity of neuronal signaling. MUT-7 acts specifically in the cytoplasm to promote siRNA biogenesis and in the nucleus to associate with CeWRN-1. The import of siRNA by the nuclear Argonaute NRDE-3 promotes the loading of the heterochromatin-binding protein HP1 homolog HPL-2 onto specific loci. This heterochromatin complex represses the gene expression of the guanylyl cyclase ODR-1 to direct olfactory plasticity in C. elegans. Our findings suggest that the exonuclease and helicase domains of human WRN may act in concert to promote RNA-dependent loading into a heterochromatin complex, and the failure of this entire process reduces plasticity in postmitotic neurons.
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