Two flagellar BAR domain proteins in Trypanosoma brucei with stage-specific regulation

0467644 - BC 2017 RIV GB eng J - Článek v odborném periodiku
Číčová, Z. - Dejung, M. - Skalický, Tomáš - Eisenhuth, N. - Hanselmann, S. - Morriswood, B. - Figueiredo, L.M. - Butter, F. - Janzen, C. J.
Two flagellar BAR domain proteins in Trypanosoma brucei with stage-specific regulation.
Scientific Reports. Roč. 6, 25 October (2016), č. článku 35826. ISSN 2045-2322. E-ISSN 2045-2322
Institucionální podpora: RVO:60077344
Klíčová slova: variant surface glycoprotein * attachment zone filament * blood stream forms * life cycle stages * paraflagellar rod * stable transformation * cell morphogenesis * ortholog groups * psi blast * membrane
Kód oboru RIV: EB - Genetika a molekulární biologie
Impakt faktor: 4.259, rok: 2016

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 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.
Trvalý link: http://hdl.handle.net/11104/0265714