Cited by 138Trypanosoma species research and implicationsBiotin and Related StudiesGenetic and Kidney Cyst Diseases

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Novel Bilobe Components in Trypanosoma brucei Identified Using Proximity-Dependent Biotinylation

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Morriswood, Brooke, Havlicek, Katharina, Demmel, Lars, Yavuz, Sevil, Sealey-Cardona, Marco, Vidilaseris, Keni, Anrather, Dorothea, Kostan, Julius, Djinović-Carugo, Kristina, Roux, Kyle J., Warren, Graham·2013·Eukaryotic Cell

DOI 10.1128/ec.00326-12PMC PMC3571296

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Abstract

The trypanosomes are a family of parasitic protists of which the African trypanosome, Trypanosoma brucei , is the best characterized. The complex and highly ordered cytoskeleton of T. brucei has been shown to play vital roles in its biology but remains difficult to study, in large part owing to the intractability of its constituent proteins. Existing methods of protein identification, such as bioinformatic analysis, generation of monoclonal antibody panels, proteomics, affinity purification, and yeast two-hybrid screens, all have drawbacks. Such deficiencies—troublesome proteins and technical limitations—are common not only to T. brucei but also to many other protists, many of which are even less well studied. Proximity-dependent biotin identification (BioID) is a recently developed technique that allows forward screens for interaction partners and near neighbors in a native environment with no requirement for solubility in nonionic detergent. As such, it is extremely well suited to the exploration of the cytoskeleton. In this project, BioID was adapted for use in T. brucei . The trypanosome bilobe, a discrete cytoskeletal structure with few known protein components, represented an excellent test subject. Use of the bilobe protein TbMORN1 as a probe resulted in the identification of seven new bilobe constituents and two new flagellum attachment zone proteins. This constitutes the first usage of BioID on a largely uncharacterized structure, and demonstrates its utility in identifying new components of such a structure. This remarkable success validates BioID as a new tool for the study of unicellular eukaryotes in particular and the eukaryotic cytoskeleton in general.

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Self-citation
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Authors: Morriswood, B., Havlicek, K., Demmel, L., Yavuz, S., Sealey-Cardona, M., Vidilaseris, K., Anrather, D., Kostan, J., Djinović-Carugo, K., Roux, K. J., & Warren, G.
Affiliations: University of Vienna (AT)
Max F. Perutz Laboratories, University of Vienna and Medical University of Vienna, Vienna, Austria
Department for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria
Sanford Research (US)
ORCID: Morriswood, Brooke
Vidilaseris, Keni
Anrather, Dorothea
Roux, Kyle J.
Venue: Eukaryotic Cell
Publisher: American Society for Microbiology
Published: 2013-02
Volume: 12
Issue: 2
Pages: 356-367
ISSN: 1535-9778 (ISSN-L)
1535-9786
DOI: 10.1128/ec.00326-12
PMC: PMC3571296
OpenAlex: W2168967957
Cited by: 138
References: 30
Citations by year: 2026: 7 · 2025: 4 · 2024: 3 · 2023: 6 · 2022: 7 · 2021: 11 · 2020: 13 · 2019: 14 · 2018: 11 · 2017: 12 · 2016: 15 · 2015: 15 · 2014: 11 · 2013: 8
FWCI: 8.35
Type: journal article
Language: en
Open access: diamond
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Eukaryotic Cell (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Epidemiology › Trypanosoma species research and implications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
Keywords: Trypanosoma brucei, cytoskeleton, proximity biotinylation, BioID, flagellum attachment zone, protein-protein interaction, protein identification, trypanosomes
MeSH terms: Cytoskeletal Proteins, Protein Binding, Trypanosoma brucei brucei, Protozoan Proteins, Biotinylation, Protein Transport, Protein Interaction Mapping

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Novel Bilobe Components in Trypanosoma brucei Identified Using Proximity-Dependent Biotinylation

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