a protein-protein interaction map of the trypanosoma brucei paraflagellar rod锥虫属的蛋白质交互地图brucei paraflagellar杆.pdfVIP
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a protein-protein interaction map of the trypanosoma brucei paraflagellar rod锥虫属的蛋白质交互地图brucei paraflagellar杆
A Protein-Protein Interaction Map of the Trypanosoma
brucei Paraflagellar Rod
Sylvain Lacomble., Neil Portman., Keith Gull*
Sir William Dunn School of Pathology and Oxford Centre for Integrative Systems Biology, University of Oxford, Oxford, United Kingdom
Abstract
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.
Citation: Lacomble S, Portman N, Gull K (2009) A Protein-Protein Interaction Map of the Trypanosoma brucei Paraflagellar Rod. PLoS ONE 4(11): e7685.
doi:10.1371/journal.pone.0007685
Editor: Adam Yuan, Temasek Life Sciences Laboratory, Singapore
Received September 2, 2009; Accepted October 12, 2009; Published November 3, 2009
Copyright: 2009 Lacomble et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits
unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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