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Title: Prolines in the α-helix confer the structural flexibility and functional integrity of importin-β
Authors: Kumeta, Masahiro  kyouindb  KAKEN_id
Konishi, Hide A.
Zhang, Wanzhen
Sakagami, Sayuri
Yoshimura, Shige H.
Author's alias: 粂田, 昌宏
小西, 秀明
坂上, 小百合
吉村, 成弘
Keywords: Importin
Molecular flexibility
Molecular structure
Nuclear transport
Issue Date: 4-Jan-2018
Publisher: The Company of Biologists
Journal title: Journal of Cell Science
Volume: 131
Issue: 1
Thesis number: jcs206326
Abstract: The karyopherin family of nuclear transport receptors is composed of a long array of amphiphilic α-helices and undergoes flexible conformational changes to pass through the hydrophobic crowding barrier of the nuclear pore. Here, we focused on the characteristic enrichment of prolines in the middle of the outer α-helices of importin-β. When these prolines were substituted with alanine, nuclear transport activity was reduced drastically in vivo and in vitro, and caused a severe defect in mitotic progression. These mutations did not alter the overall folding of the helical repeat or affect its interaction with cargo or the regulatory factor Ran. However, in vitro and in silico analyses revealed that the mutant lost structural flexibility and could not undergo rapid conformational changes when transferring from a hydrophilic to hydrophobic environment or vice versa. These findings reveal the essential roles of prolines in ensuring the structural flexibility and functional integrity of karyopherins.
Rights: © 2018. Published by The Company of Biologists Ltd.
The full-text file will be made open to the public on 04 January 2019 in accordance with publisher's 'Terms and Conditions for Self-Archiving'.
DOI(Published Version): 10.1242/jcs.206326
PubMed ID: 29142102
Appears in Collections:Journal Articles

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