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. 2013 Dec 1;24(23):3689–3696. doi: 10.1091/mbc.E13-06-0310

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© 2013 Dean and Mitchell. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 1: — ODA10p is a conserved coiled-coil protein. (A) A Coomassie-stained gel (top) and Western blot (bottom), probed with an antibody against HA epitope, of equally loaded (by cell number) whole-cell samples of oda10-2,ODA10HA and oda10-2 cells show expression of ODA10HAp in a strain with rescued beat frequency. (B) A Coomassie-stained gel (top) and western blot (bottom), probed with antibodies against HA epitope and IC2, of flagellar samples of mutant (oda10-2), wild type (137c), and rescued transformants (oda10-2,ODA10HA 1-9) show restored assembly of outer dynein arms to wild-type levels in transformant cells expressing the highest levels of ODA10HAp. (C) The distribution of predicted coiled-coil domains of ODA1p, ODA3p, ODA5p, and ODA10p. (D) All homologues of ODA10p and of three Chlamydomonas ODA10p paralogues (ODA5p, ODA1p [ = DC2], ODA3p [ = DC1]) in an alga (Micromonas), a basal chordate (Ciona), a fish (Danio), and a mammal (Mus) were aligned, and an unrooted tree was generated to display relative sequence similarities. Green background highlights homologues of ODA1p; yellow background highlights homologues of ODA10p. Protein sequences used in the alignments that are not given in the figure were Q8CDV6 (ccdc63), AAI60348 (ccdc114), AAH57069 (ccdc151), NP_001027646 (Ciona p66), NP_001072015 (Ciona IC4), NP_001071888 (Ciona IC5), AAC49732 (ODA3), AAK72125 (ODA1), AAS10183 (ODA5), and AGW18228 (ODA10).