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LdFlabarin, a New BAR Domain Membrane Protein of Leishmania Flagellum

by Thonnus, Magali , Metzler, Christelle , Sahin, Annelise , Tetaud, Emmanuel , Lefebvre, Michèle , Blancard, Corinne , Sauvanet, Cécile , Salin, Bénédicte , Espiau, Benoît , Merlin, Gilles , Boissier, Fanny

in Acylation / Amino acids / Base Sequence / Biosynthesis / Cellular Biology / Computational Biology / Deoxyribonucleic acid / Dismantling / DNA / Evolution, Molecular / Flagella / Flagella - genetics / Flagella - metabolism / Flagella - ultrastructure / Genomes / Laboratories / Leishmania / Leishmania - genetics / Leishmania - metabolism / Life cycle engineering / Life cycles / Life Sciences / Liposomes / Liposomes - metabolism / Membrane proteins / Membrane Proteins - genetics / Membrane Proteins - metabolism / Membranes / Molecular Sequence Data / Mutagenesis, Site-Directed / Parasites / Phylogeny / Protein Binding / Protein Structure, Tertiary / Proteins / RNA polymerase / Sequence Analysis, DNA / Site-directed mutagenesis / Trypanosoma brucei

2013

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LdFlabarin, a New BAR Domain Membrane Protein of Leishmania Flagellum

2013

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LdFlabarin, a New BAR Domain Membrane Protein of Leishmania Flagellum

2013

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Journal Article

LdFlabarin, a New BAR Domain Membrane Protein of Leishmania Flagellum

Thonnus, Magali,

Metzler, Christelle,

Sahin, Annelise,

Tetaud, Emmanuel,

Lefebvre, Michèle,

Blancard, Corinne,

Sauvanet, Cécile,

Salin, Bénédicte,

Espiau, Benoît,

Merlin, Gilles,

Boissier, Fanny

2013

Overview

During the Leishmania life cycle, the flagellum undergoes successive assembly and disassembly of hundreds of proteins. Understanding these processes necessitates the study of individual components. Here, we investigated LdFlabarin, an uncharacterized L. donovani flagellar protein. The gene is conserved within the Leishmania genus and orthologous genes only exist in the Trypanosoma genus. LdFlabarin associates with the flagellar plasma membrane, extending from the base to the tip of the flagellum as a helicoidal structure. Site-directed mutagenesis, deletions and chimera constructs showed that LdFlabarin flagellar addressing necessitates three determinants: an N-terminal potential acylation site and a central BAR domain for membrane targeting and the C-terminal domain for flagellar specificity. In vitro, the protein spontaneously associates with liposomes, triggering tubule formation, which suggests a structural/morphogenetic function. LdFlabarin is the first characterized Leishmania BAR domain protein, and the first flagellum-specific BAR domain protein.

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Publisher

Public Library of Science,Public Library of Science (PLoS)

Subject

/ Computational Biology

/ Deoxyribonucleic acid