Piwi Nuclear Localization and Its Regulatory Mechanism in Drosophila Ovarian Somatic Cells
| Autor: | Asuka Ogai, Haruhiko Siomi, Mikiko C. Siomi, Soichiro Yamanaka, Kazumichi M. Nishida, Lumi Negishi, Ryu Yashiro, Kaede Fujii, Haruna Yamashiro, Yukiko Murota |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Transposable element endocrine system Somatic cell Nuclear Localization Signals Piwi-interacting RNA Biology General Biochemistry Genetics and Molecular Biology Cell Line 03 medical and health sciences 0302 clinical medicine medicine NLS Animals Drosophila Proteins Amino Acid Sequence Cell Nucleus urogenital system Ovary RNA Cell biology 030104 developmental biology medicine.anatomical_structure Drosophila melanogaster Cytoplasm Argonaute Proteins Female Nucleus 030217 neurology & neurosurgery Nuclear localization sequence |
| Zdroj: | Cell reports. 23(12) |
| ISSN: | 2211-1247 |
| Popis: | In Drosophila ovarian somatic cells (OSCs), Piwi represses transposons transcriptionally to maintain genome integrity. Piwi nuclear localization requires the N terminus and PIWI-interacting RNA (piRNA) loading of Piwi. However, the underlying mechanism remains unknown. Here, we show that Importinα (Impα) plays a pivotal role in Piwi nuclear localization and that Piwi has a bipartite nuclear localization signal (NLS). Impα2 and Impα3 are highly expressed in OSCs, whereas Impα1 is the least expressed. Loss of Impα2 or Impα3 forces Piwi to be cytoplasmic, which is rectified by overexpression of any Impα members. Extension of Piwi-NLS with an additional Piwi-NLS leads Piwi to be imported to the nucleus in a piRNA-independent manner, whereas replacement of Piwi-NLS with SV40-NLS fails. Limited proteolysis analysis suggests that piRNA loading onto Piwi triggers conformational change, exposing the N terminus to the environment. These results suggest that Piwi autoregulates its nuclear localization by exposing the NLS to Impα upon piRNA loading. |
| Databáze: | OpenAIRE |
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