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Two flagellar BAR domain proteins in Trypanosoma brucei with stage-specific regulation
Please always quote using this URN: urn:nbn:de:bvb:20-opus-181021
- Trypanosomes are masters of adaptation to different host environments during their complex life cycle. Large-scale proteomic approaches provide information on changes at the cellular level, and in a systematic way. However, detailed work on single components is necessary to understand the adaptation mechanisms on a molecular level. Here, we have performed a detailed characterization of a bloodstream form (BSF) stage-specific putative flagellar host adaptation factor Tb927.11.2400, identified previously in a SILAC-based comparative proteomeTrypanosomes are masters of adaptation to different host environments during their complex life cycle. Large-scale proteomic approaches provide information on changes at the cellular level, and in a systematic way. However, detailed work on single components is necessary to understand the adaptation mechanisms on a molecular level. Here, we have performed a detailed characterization of a bloodstream form (BSF) stage-specific putative flagellar host adaptation factor Tb927.11.2400, identified previously in a SILAC-based comparative proteome study. Tb927.11.2400 shares 38% amino acid identity with TbFlabarin (Tb927.11.2410), a procyclic form (PCF) stage-specific flagellar BAR domain protein. We named Tb927.11.2400 TbFlabarin-like (TbFlabarinL), and demonstrate that it originates from a gene duplication event, which occurred in the African trypanosomes. TbFlabarinL is not essential for the growth of the parasites under cell culture conditions and it is dispensable for developmental differentiation from BSF to the PCF in vitro. We generated TbFlabarinL-specific antibodies, and showed that it localizes in the flagellum. Co-immunoprecipitation experiments together with a biochemical cell fractionation suggest a dual association of TbFlabarinL with the flagellar membrane and the components of the paraflagellar rod.…
Author: | Zdenka Cicova, Mario Dejung, Tomas Skalicky, Nicole Eisenhuth, Steffen Hanselmann, Brooke Morriswood, Luisa M. Figueiredo, Falk Butter, Christian J. Janzen |
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URN: | urn:nbn:de:bvb:20-opus-181021 |
Document Type: | Journal article |
Faculties: | Fakultät für Biologie / Julius-von-Sachs-Institut für Biowissenschaften |
Language: | English |
Parent Title (English): | Scientific Reports |
Year of Completion: | 2016 |
Volume: | 6 |
Article Number: | 35826 |
Source: | Scientific Reports 2016, 6:35826. DOI: 10.1038/srep35826 |
DOI: | https://doi.org/10.1038/srep35826 |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 579 Mikroorganismen, Pilze, Algen |
Tag: | Trypanosoma brucei; parasite biology; protein translocation |
Release Date: | 2021/03/08 |
Licence (German): | CC BY: Creative-Commons-Lizenz: Namensnennung 4.0 International |