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Protein-protein interactions between intermediate chains and the docking complex of Chlamydomonas flagellar outer arm dynein.

ABSTRACT: 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.

SUBMITTER: Ide T

PROVIDER: S-EPMC3746069 | biostudies-other | 2013 Jul

REPOSITORIES: biostudies-other

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Protein-protein interactions between intermediate chains and the docking complex of Chlamydomonas flagellar outer arm dynein.

Ide Takahiro T Owa Mikito M King Stephen M SM Kamiya Ritsu R Wakabayashi Ken-ichi K

FEBS letters 20130606 14

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 ...[more]

PMID: 23747306

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