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Post-translational modification of proteins as a regulatory mechanism in the nuclear VSG-ES body

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The importance of nuclear bodies and the three-dimensional organization of chromosomes in the regulation of gene expression have recently become evident in eukaryotes. In Trypanosoma brucei the main surface-protein genes (VSG and Procyclin) are transcribed by the highly compartmentalized RNA polymerase I and undergo distinct transcriptional activation or downregulation during developmental differentiation. Furthermore, the infective bloodstream form of the parasite undergoes antigenic variation, displaying sequentially different types of VSG by mono-allelic expression. Previously, we proposed that the recruitment of a single Variant Surface Glycoprotein Expression Site (VSG-ES) telomeric locus to a discrete, RNA pol I-containing nuclear Body (ESB) defines the mechanism responsible for VSG mono-allelic expression.

The aim of the research in our group is to identify the molecular mechanisms involved in nuclear body coherence and stability. Over the last few years we have searched for molecules involved in ESB nuclear body regulation and have identified two classes of post-translational protein modifications related to ESB stability and coherency. These modifications include the Small Ubiquitin-like Modifier (SUMO) and protein phosphorylation. Importantly, we have identified two proteins responsible for these modifications: the SP-RING SUMO ligase we named SIZ1 and the protein kinase TOR family.

This talk is part of the Parasitology Seminars series.

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