Abstract
ABSTRACTThe basal body shares similar architecture with centrioles in animals and is involved in nucleating flagellar axonemal microtubules in flagellated eukaryotes. The early-branching Trypanosoma brucei possesses a motile flagellum nucleated from the basal body that consists of a mature basal body and an adjacent pro-basal body. Little is known about the basal body proteome and its roles in basal body biogenesis and flagellar axoneme assembly in T. brucei. Here, we report the identification of 14 conserved centriole/basal body protein homologs and 25 trypanosome-specific basal body proteins. These proteins localize to distinct subdomains of the basal body, and several of them form a ring-like structure surrounding the basal body barrel. Functional characterization of representative basal body proteins revealed distinct roles in basal body duplication/separation and flagellar axoneme assembly. Overall, this work identified novel proteins required for basal body duplication and separation and uncovered new functions of conserved basal body proteins in basal body duplication and separation, highlighting an unusual mechanism of basal body biogenesis and inheritance in this early divergent eukaryote.
Highlights
IMPORTANCE The basal body in the early-branching protozoan Trypanosoma brucei nucleates flagellum assembly and regulates organelle segregation, cell morphogenesis, and cell division
SAS-6 and BLD10/CEP135 are among the 14 ancestral centriole core components that have been identified in 45 organisms [3] and, together with SAS-4/CPAP, they are considered the core ancestral module involved in centriole/ basal body biogenesis [4]
A number of evolutionarily conserved centriole/basal body protein homologs have been identified in T. brucei by bioinformatics analyses [3, 4], many basal body proteins from Chlamydomonas reinhardtii and centrosome proteins from humans have not been used to search for T. brucei homologs
Summary
IMPORTANCE The basal body in the early-branching protozoan Trypanosoma brucei nucleates flagellum assembly and regulates organelle segregation, cell morphogenesis, and cell division. We identify 14 conserved basal body proteins and 25 trypanosome-specific basal body proteins via bioinformatics, localization-based screening, and proximity-dependent biotin identification. T. brucei appears to lack many conserved basal body protein homologs [3, 4] and does not employ the conserved polo-like kinase-mediated signaling pathway to govern basal body biogenesis [11, 15] These findings suggest an unusual mechanism for basal body duplication in T. brucei and necessitate further exploration of basal body proteome and discovery of trypanosome-specific regulators. We carried out bioinformatics analysis to identify the evolutionarily conserved centriole/basal body protein homologs in T. brucei and performed proximitydependent biotin identification (BioID) [16] and subcellular localization-based screening to identify trypanosome-specific basal body proteins. This work represents a major step forward toward the determination of T. brucei basal body proteome and the understanding of basal body duplication, and it highlights the essential involvement of trypanosome-specific proteins in regulating basal body duplication and separation
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