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  1. B100 理学部/理学研究科
  2. B100a 雑誌掲載論文
  3. 学術雑誌

Crystal structure of the Xpo1p nuclear export complex bound to the SxFG/PxFG repeats of the nucleoporin Nup42p

http://hdl.handle.net/2237/27282
http://hdl.handle.net/2237/27282
625e2604-0916-4fce-8a6f-8c07d7826347
名前 / ファイル ライセンス アクション
koyama2017GenesCells_accepted_for_depository3.pdf koyama2017GenesCells_accepted_for_depository3.pdf ファイル公開:2018/10/01 (7.4 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2018-01-18
タイトル
タイトル Crystal structure of the Xpo1p nuclear export complex bound to the SxFG/PxFG repeats of the nucleoporin Nup42p
言語 en
著者 Koyama, Masako

× Koyama, Masako

WEKO 74748

en Koyama, Masako

Search repository
Hirano, Hidemi

× Hirano, Hidemi

WEKO 74749

en Hirano, Hidemi

Search repository
Shirai, Natsuki

× Shirai, Natsuki

WEKO 74750

en Shirai, Natsuki

Search repository
Matsuura, Yoshiyuki

× Matsuura, Yoshiyuki

WEKO 74751

en Matsuura, Yoshiyuki

Search repository
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利
言語 en
権利情報 This is the peer reviewed version of the following article: [Koyama, M., Hirano, H., Shirai, N. and Matsuura, Y. (2017), Crystal structure of the Xpo1p nuclear export complex bound to the SxFG/PxFG repeats of the nucleoporin Nup42p. Genes Cells, 22: 861–875. doi:10.1111/gtc.12520], which has been published in final form at [http://doi.org/10.1002/pro.3244]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
抄録
内容記述 Xpo1p (yeast CRM1) is the major nuclear export receptor that carries a plethora of proteins and ribonucleoproteins from the nucleus to cytoplasm. The passage of the Xpo1p nuclear export complex through nuclear pore complexes (NPCs) is facilitated by interactions with nucleoporins (Nups) containing extensive repeats of phenylalanine–glycine (so-called FG repeats), although the precise role of each Nup in the nuclear export reaction remains incompletely understood. Here we report structural and biochemical characterization of the interactions between the Xpo1p nuclear export complex and the FG repeats of Nup42p, a nucleoporin localized at the cytoplasmic face of yeast NPCs and has characteristic SxFG/PxFG sequence repeat motif. The crystal structure of Xpo1p-PKI-Nup42p-Gsp1p-GTP complex identified three binding sites for the SxFG/PxFG repeats on HEAT repeats 14–20 of Xpo1p. Mutational analyses of Nup42p showed that the conserved serines and prolines in the SxFG/PxFG repeats contribute to Xpo1p-Nup42p binding. Our structural and biochemical data suggest that SxFG/PxFG-Nups such as Nup42p and Nup159p at the cytoplasmic face of NPCs provide high-affinity docking sites for the Xpo1p nuclear export complex in the terminal stage of NPC passage and that subsequent disassembly of the nuclear export complex facilitates recycling of free Xpo1p back to the nucleus.
言語 en
内容記述タイプ Abstract
出版者
言語 en
出版者 Wiley
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1111/gtc.12520
ISSN
収録物識別子タイプ PISSN
収録物識別子 1356-9597
書誌情報 en : Genes to Cells

巻 22, 号 10, p. 861-875, 発行日 2017-10
著者版フラグ
値 author
URI
識別子 http://doi.org/10.1111/gtc.12520
識別子タイプ DOI
URI
識別子 http://hdl.handle.net/2237/27282
識別子タイプ HDL
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