A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.

We have conducted a protein interaction study of components within a specific sub-compartment of a eukaryotic flagellum. The trypanosome flagellum contains a para-crystalline extra-axonemal structure termed the paraflagellar rod (PFR) with around forty identified components. We have used a Gateway c...

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Main Authors: Sylvain Lacomble, Neil Portman, Keith Gull
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2009-11-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2766642?pdf=render
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author Sylvain Lacomble
Neil Portman
Keith Gull
author_facet Sylvain Lacomble
Neil Portman
Keith Gull
author_sort Sylvain Lacomble
collection DOAJ
description We have conducted a protein interaction study of components within a specific sub-compartment of a eukaryotic flagellum. The trypanosome flagellum contains a para-crystalline extra-axonemal structure termed the paraflagellar rod (PFR) with around forty identified components. We have used a Gateway cloning approach coupled with yeast two-hybrid, RNAi and 2D DiGE to define a protein-protein interaction network taking place in this structure. We define two clusters of interactions; the first being characterised by two proteins with a shared domain which is not sufficient for maintaining the interaction. The other cohort is populated by eight proteins, a number of which possess a PFR domain and sub-populations of this network exhibit dependency relationships. Finally, we provide clues as to the structural organisation of the PFR at the molecular level. This multi-strand approach shows that protein interactome data can be generated for insoluble protein complexes.
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spelling doaj.art-3e88c5df4697477da7d8b5b85dea00032022-12-22T03:58:44ZengPublic Library of Science (PLoS)PLoS ONE1932-62032009-11-01411e768510.1371/journal.pone.0007685A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.Sylvain LacombleNeil PortmanKeith GullWe have conducted a protein interaction study of components within a specific sub-compartment of a eukaryotic flagellum. The trypanosome flagellum contains a para-crystalline extra-axonemal structure termed the paraflagellar rod (PFR) with around forty identified components. We have used a Gateway cloning approach coupled with yeast two-hybrid, RNAi and 2D DiGE to define a protein-protein interaction network taking place in this structure. We define two clusters of interactions; the first being characterised by two proteins with a shared domain which is not sufficient for maintaining the interaction. The other cohort is populated by eight proteins, a number of which possess a PFR domain and sub-populations of this network exhibit dependency relationships. Finally, we provide clues as to the structural organisation of the PFR at the molecular level. This multi-strand approach shows that protein interactome data can be generated for insoluble protein complexes.http://europepmc.org/articles/PMC2766642?pdf=render
spellingShingle Sylvain Lacomble
Neil Portman
Keith Gull
A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.
PLoS ONE
title A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.
title_full A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.
title_fullStr A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.
title_full_unstemmed A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.
title_short A protein-protein interaction map of the Trypanosoma brucei paraflagellar rod.
title_sort protein protein interaction map of the trypanosoma brucei paraflagellar rod
url http://europepmc.org/articles/PMC2766642?pdf=render
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