An Argonaute Transports siRNAs from the Cytoplasm to the Nucleus

Author:

Guang Shouhong1234,Bochner Aaron F.1234,Pavelec Derek M.1234,Burkhart Kirk B.1234,Harding Sandra1234,Lachowiec Jennifer1234,Kennedy Scott1234

Affiliation:

1. Department of Pharmacology, University of Wisconsin–Madison, Madison, WI 53706, USA.

2. Program in Cellular and Molecular Biology, University of Wisconsin–Madison, Madison, WI 53706, USA.

3. Program in Molecular and Cellular Pharmacology, University of Wisconsin–Madison, Madison, WI 53706, USA.

4. Department of Genetics, University of Wisconsin–Madison, Madison, WI 53706, USA.

Abstract

Ribonucleoprotein complexes consisting of Argonaute-like proteins and small regulatory RNAs function in a wide range of biological processes. Many of these small regulatory RNAs are predicted to act, at least in part, within the nucleus. We conducted a genetic screen to identify factors essential for RNA interference (RNAi) in nuclei of Caenorhabditis elegans and identified the Argonaute protein NRDE-3. In the absence of small interfering RNAs (siRNAs), NRDE-3 resides in the cytoplasm. NRDE-3 binds siRNAs generated by RNA-dependent RNA polymerases acting on messenger RNA templates in the cytoplasm and redistributes to the nucleus. Nuclear redistribution of NRDE-3 requires a functional nuclear localization signal, is required for nuclear RNAi, and results in NRDE-3 association with nuclear-localized nascent transcripts. Thus, specific Argonaute proteins can transport specific classes of small regulatory RNAs to distinct cellular compartments to regulate gene expression.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference21 articles.

1. Materials and methods are available as supporting material on Science Online.

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3. Single-letter abbreviations for the amino acid residues are as follows: A Ala; C Cys; D Asp; E Glu; F Phe; G Gly; H His; I Ile; K Lys; L Leu; M Met; N Asn; P Pro; Q Gln; R Arg; S Ser; T Thr; V Val; W Trp; and Y Tyr.

4. Interacting endogenous and exogenous RNAi pathways in Caenorhabditis elegans

5. Functional Proteomics Reveals the Biochemical Niche of C. elegans DCR-1 in Multiple Small-RNA-Mediated Pathways

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