Basalin is an evolutionarily unconstrained protein revealed via a conserved role in flagellum basal plate function

ELife
Samuel DeanKeith Gull

Abstract

Most motile flagella have an axoneme that contains nine outer microtubule doublets and a central pair (CP) of microtubules. The CP coordinates the flagellar beat and defects in CP projections are associated with motility defects and human disease. The CP nucleate near a 'basal plate' at the distal end of the transition zone (TZ). Here, we show that the trypanosome TZ protein 'basalin' is essential for building the basal plate, and its loss is associated with CP nucleation defects, inefficient recruitment of CP assembly factors to the TZ, and flagellum paralysis. Guided by synteny, we identified a highly divergent basalin ortholog in the related Leishmania species. Basalins are predicted to be highly unstructured, suggesting they may act as 'hubs' facilitating many protein-protein interactions. This raises the general concept that proteins involved in cytoskeletal functions and appearing organism-specific, may have highly divergent and cryptic orthologs in other species.

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Citations

Jan 17, 2020·Cellular Microbiology·Eloïse Bertiaux, Philippe Bastin
Nov 1, 2020·Trends in Parasitology·Anzhelika ButenkoJulius Lukeš
Apr 4, 2021·International Journal of Molecular Sciences·Zuzanna SamselEwa Joachimiak
Jul 21, 2021·Journal of Cell Science·Nina Schweizer, Jens Lüders

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Methods Mentioned

BETA
transmission electron microscopy
fluorescence microscopy
PCR
electron microscopy

Software Mentioned

BLASTP
FIJI
Quick2D
TriTrypDB
Adobe Illustrator
OrthoMCL
HHpred
BLAST
Orthofinder
TAGit

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