Aub and Ago3 are recruited to nuage through two mechanisms to form a ping-pong complex assembled by Krimper Journal Article
| Authors: | Webster, A.; Li, S.; Hur, J. K.; Wachsmuth, M.; Bois, J. S.; Perkins, E. M.; Patel, D. J.; Aravin, A. A. |
| Article Title: | Aub and Ago3 are recruited to nuage through two mechanisms to form a ping-pong complex assembled by Krimper |
| Abstract: | In Drosophila, two Piwi proteins, Aubergine (Aub) and Argonaute-3 (Ago3), localize to perinuclear "nuage" granules and use guide piRNAs to target and destroy transposable element transcripts. We find that Aub and Ago3 are recruited to nuage by two different mechanisms. Aub requires a piRNA guide for nuage recruitment, indicating that its localization depends on recognition of RNA targets. Ago3 is recruited to nuage independently of a piRNA cargo and relies on interaction with Krimper, a stable component of nuage that is able to aggregate in the absence of other nuage proteins. We show that Krimper interacts directly with Aub and Ago3 to coordinate the assembly of the ping-pong piRNA processing (4P) complex. Symmetrical dimethylated arginines are required for Aub to interact with Krimper, but they are dispensable for Ago3 to bind Krimper. Our study reveals a multi-step process responsible for the assembly and function of nuage complexes in piRNA-guided transposon repression. © 2015 Elsevier Inc. |
| Keywords: | controlled study; unclassified drug; methylation; nonhuman; protein localization; complex formation; protein protein interaction; cell membrane; argonaute protein; arginine; piwi interacting rna; protein rna binding; piwi protein; aubergine protein; solanum melongena; article; argonaute 3 protein; krimper protein; nuage |
| Journal Title: | Molecular Cell |
| Volume: | 59 |
| Issue: | 4 |
| ISSN: | 1097-2765 |
| Publisher: | Cell Press |
| Date Published: | 2015-08-20 |
| Start Page: | 564 |
| End Page: | 575 |
| Language: | English |
| DOI: | 10.1016/j.molcel.2015.07.017 |
| PROVIDER: | scopus |
| PMCID: | PMC4545750 |
| PUBMED: | 26295961 |
| DOI/URL: | |
| Notes: | Export Date: 2 September 2015 -- Source: Scopus |
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