若林 憲一
   所属   京都産業大学  生命科学部 産業生命科学科
   職種   教授
言語種別 英語
発行・発表の年月 2013/07
形態種別 研究論文
査読 査読あり
標題 Protein-protein interactions between intermediate chains and the docking complex of Chlamydomonas flagellar outer arm dynein
執筆形態 その他
掲載誌名 FEBS LETTERS
出版社・発行元 ELSEVIER SCIENCE BV
巻・号・頁 587(14),pp.2143-2149
担当区分 責任著者
著者・共著者 Takahiro Ide,Mikito Owa,Stephen M. King,Ritsu Kamiya,Ken-ichi Wakabayashi
概要 Outer arm dynein (OAD) is bound to specific loci on outer-doublet-microtubules by interactions at two sites: via intermediate chain 1 (IC1) and the outer dynein arm docking complex (ODA-DC). Studies using Chlamydomonas mutants have suggested that the individual sites have rather weak affinities for microtubules, and therefore strong OAD attachment to microtubules is achieved by their cooperation. To test this idea, we examined interactions between IC1, IC2 (another intermediate chain) and ODA-DC using recombinant proteins. Recombinant IC1 and IC2 were found to form a 1:1 complex, and this complex associated with ODA-DC in vitro. Binding of IC1 to mutant axonemes revealed that there are specific binding sites for IC1. From these data, we propose a novel model of OAD-outer doublet association.
Structured summary of protein interactions:
IC2 physically interacts with DC2 and DC1 by anti bait coimmunoprecipitation (View interaction)
DC2 physically interacts with IC2 and IC1 by anti bait coimmunoprecipitation (View interaction)
IC2 and IC1 physically interact by cross-linking study (View interaction)
IC2 and DC1 physically interact by cross-linking study (View interaction)
DC2 and DC1 physically interact by cross-linking study (View Interaction: 1, 2)
DC1 and IC1 physically interact by cross-linking study (View interaction)
IC2 binds to IC1 by anti bait coimmunoprecipitation (View interaction)
IC2, DC1 and DC2 physically interact by cross-linking study (View interaction)
DC2, IC1 and DC1 physically interact by cross-linking study (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
DOI 10.1016/j.febslet.2013.05.058
ISSN 0014-5793
PMID 23747306