Proteome turnover in the bloodstream and procyclic forms of Trypanosoma brucei measured by quantitative proteomics
Open Access
- 9 October 2019
- journal article
- Published by F1000 Research Ltd in Wellcome Open Research
Abstract
Background: Cellular proteins vary significantly in both abundance and turnover rates. These parameters depend upon their rates of synthesis and degradation and it is useful to have access to data on protein turnover rates when, for example, designing genetic knock-down experiments or assessing the potential usefulness of covalent enzyme inhibitors. Little is known about the nature and regulation of protein turnover in Trypanosoma brucei, the etiological agent of human and animal African trypanosomiasis. Methods: To establish baseline data on T. brucei proteome turnover, a Stable Isotope Labelling with Amino acids in Cell culture (SILAC)-based mass spectrometry analysis was performed to reveal the synthesis and degradation profiles for thousands of proteins in the bloodstream and procyclic forms of this parasite. Results: This analysis revealed a slower average turnover rate of the procyclic form proteome relative to the bloodstream proteome. As expected, many of the proteins with the fastest turnover rates have functions in the cell cycle and in the regulation of cytokinesis in both bloodstream and procyclic forms. Moreover, the cellular localization of T. brucei proteins correlates with their turnover, with mitochondrial and glycosomal proteins exhibiting slower than average turnover rates. Conclusions: The intention of this study is to provide the trypanosome research community with a resource for protein turnover data for any protein or group of proteins. To this end, bioinformatic analyses of these data are made available via an open-access web resource with data visualization functions.Funding Information
- Wellcome Trust (101842)
- Wellcome Trust (050662.D10, 090944, 097045)
This publication has 58 references indexed in Scilit:
- The Regulation of Trypanosome Gene Expression by RNA-Binding ProteinsPLoS Pathogens, 2013
- Global Quantitative SILAC Phosphoproteomics Reveals Differential Phosphorylation Is Widespread between the Procyclic and Bloodstream Form Lifecycle Stages of Trypanosoma bruceiJournal of Proteome Research, 2013
- Comparative Proteomics of Two Life Cycle Stages of Stable Isotope-labeled Trypanosoma brucei Reveals Novel Components of the Parasite's Host Adaptation MachineryMolecular & Cellular Proteomics, 2013
- Comparative SILAC Proteomic Analysis of Trypanosoma brucei Bloodstream and Procyclic Lifecycle StagesPLOS ONE, 2012
- A Quantitative Spatial Proteomics Analysis of Proteome Turnover in Human CellsMolecular & Cellular Proteomics, 2012
- Ubiquitylation and Developmental Regulation of Invariant Surface Protein Expression in TrypanosomesEukaryotic Cell, 2011
- The SILAC Fly Allows for Accurate Protein Quantification in VivoMolecular & Cellular Proteomics, 2010
- Genome-wide in silico screen for CCCH-type zinc finger proteins of Trypanosoma brucei, Trypanosoma cruzi and Leishmania majorBMC Genomics, 2010
- TriTrypDB: a functional genomic resource for the TrypanosomatidaeNucleic Acids Research, 2009
- MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantificationNature Biotechnology, 2008