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Fig. 5. TbCMF 9 and TbCMF 76b are part of a novel family of axonemal stabilizing proteins. Transmission EM images of flagella from the indicated TbCMF mutants. (A-C) Knockdown of TbCMF 5 does not significantly perturb the axoneme or PFR structure including the orientation of central pair microtubules. (D-F) TbCMF 9 knockdown causes a range of defects in outer-doublet arrangement. Axonemes ranged from outer doublets falling away from the axoneme (D, arrow), to groups of doublets that are completely separated from the axoneme (E, arrow), to split `hemi-axonemes', in which half of the axoneme has twisted around to a piggyback arrangement on the other half (F). This range of structural defects was observed in 44% of sections, 68% displayed doublets in disarray and 32% displayed a piggyback configuration. A total of 100 sections were examined. (G-I) Knockdown of TbCMF 76b, a protein related to TbCMF 9, results in similar ultrastructural defects. These are observed in 
40% of sections, 81% of which show aberrant outer-doublet arrangement and 19% show the hemi-axoneme arrangement. A total of 75 sections were examined. (J) Longitudinal sections of TbCMF 9 and 76b flagella. Doublets that have lost their linkages with the rest of the doublets bow out from the axoneme (arrows). Longitudinal images were taken at the same time point as the cross-sections shown in A-I.
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