4.6 Article

The distinctive flagellar proteome of Euglena gracilis illuminates the complexities of protistan flagella adaptation

Journal

NEW PHYTOLOGIST
Volume 232, Issue 3, Pages 1323-1336

Publisher

WILEY
DOI: 10.1111/nph.17638

Keywords

cilia; Euglena; evolution; flagella; pellicle; proteomics

Categories

Funding

  1. Wellcome Trust [204697/Z/16/Z]
  2. Medical Research Council [MR/P009018/1]
  3. Czech Science Foundation [18-15962S]
  4. ERC CZ [LL1601, OPVVV 16_019/0000759]
  5. Gordon and Betty Moore Foundation
  6. MRC [MR/P009018/1] Funding Source: UKRI

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Through proteomic analysis of the flagella of Euglena gracilis, unexpected similarities with mammalian flagella and a vast array of signal transduction components coordinating motility were identified. The significant adaptations within the flagellum of E. gracilis, linked to its highly flexible lifestyle, were also revealed.
The eukaryotic flagellum/cilium is a prominent organelle with conserved structure and diverse functions. Euglena gracilis, a photosynthetic and highly adaptable protist, employs its flagella for both locomotion and environmental sensing. Using proteomics of isolated E. gracilis flagella we identify nearly 1700 protein groups, which challenges previous estimates of the protein complexity of motile eukaryotic flagella. We not only identified several unexpected similarities shared with mammalian flagella, including an entire glycolytic pathway and proteasome, but also document a vast array of flagella-based signal transduction components that coordinate gravitaxis and phototactic motility. By contrast, the pellicle was found to consist of > 900 protein groups, containing additional structural and signalling components. Our data identify significant adaptations within the E. gracilis flagellum, many of which are clearly linked to the highly flexible lifestyle.

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