RecQ5 Protein Translocation into the Nucleus by a Nuclear Localization Signal
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- Sakurai Haruna
- Division of Biochemistry, Graduate School of Pharmaceutical Sciences, Setsunan University
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- Tsutsui Ayaka
- Division of Biochemistry, Graduate School of Pharmaceutical Sciences, Setsunan University
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- Higashi Takahiro
- Division of Biochemistry, Graduate School of Pharmaceutical Sciences, Setsunan University
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- Azuma Rika
- Division of Biochemistry, Graduate School of Pharmaceutical Sciences, Setsunan University
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- Ito Fumiaki
- Division of Biochemistry, Graduate School of Pharmaceutical Sciences, Setsunan University
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- Kawasaki Katsumi
- Division of Biochemistry, Graduate School of Pharmaceutical Sciences, Setsunan University Division of Molecular Biology, Department of Life Science, Faculty of Science and Engineering, Setsunan University
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RecQ5, a member of the RecQ helicase family, maintains genome stability via participation in many DNA metabolic processes including DNA repair, DNA resolution, and RNA transcription, processes occurring in the nucleus. Previously, we reported that RecQ5 and Rad51, also involved in DNA repair, become co-localized in nuclei when co-expressed in cultured cells. Nuclear localization of RecQ5 appears to be important for cellular function along with Rad51. However, little is known about the nuclear localization of RecQ5. Here, we generated enhanced green fluorescent protein (EGFP)-tagged RecQ5 transgenic flies and analyzed localization of this protein in early embryos by live imaging. In syncytial embryos, RecQ5 was localized synchronously in interphase nuclei, and spread repeatedly over the embryos in mitosis. Thus, RecQ5 was transported into nuclei at the early interphase. Furthermore, we examined the subcellular localization of a series of truncated forms of Drosophila RecQ5 in cultured cells to determine the nuclear localization signal (NLS). Entire coding or deleted RecQ5 sequences of various sizes were ligated into EGFP vectors, which were then used to transfect cultured Drosophila cells. The region responsible for nuclear localization of Drosophila RecQ5 contained a short stretch of positively charged basic amino acids, 2 of which were particularly important for the nuclear localization. This stretch was sufficient for nuclear localization when fused with EGFP. Although the NLS of Drosophila RecQ5 was distinct from that of human RECQL5 in terms of position and amino acid sequence, this fly RecQ5 protein was translocated into the nucleus by an NLS.
収録刊行物
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- Biological & Pharmaceutical Bulletin
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Biological & Pharmaceutical Bulletin 36 (7), 1159-1166, 2013
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390001204632547712
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- NII論文ID
- 130003361476
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- NII書誌ID
- AA10885497
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- COI
- 1:STN:280:DC%2BC3sjmsVKlsA%3D%3D
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- ISSN
- 13475215
- 09186158
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- NDL書誌ID
- 024644699
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- PubMed
- 23811565
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 使用不可