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SUMMARY:Post-translational modification of proteins as a regulatory mechan
 ism in the nuclear VSG-ES body - Dr Miguel Navarro\,  CSIC (Spanish Nation
 al Reserach Council)
DTSTART:20130307T170000Z
DTEND:20130307T180000Z
UID:TALK43681@talks.cam.ac.uk
CONTACT:Tracey Brown
DESCRIPTION:The importance of nuclear bodies and the three-dimensional org
 anization of chromosomes in the regulation of gene expression have recentl
 y become evident in eukaryotes. In Trypanosoma brucei the main surface-pro
 tein genes (VSG and Procyclin) are transcribed by the highly compartmental
 ized RNA polymerase I and undergo distinct transcriptional activation or d
 ownregulation during developmental differentiation. Furthermore\, the infe
 ctive bloodstream form of the parasite undergoes antigenic variation\, dis
 playing sequentially different types of VSG by mono-allelic expression. Pr
 eviously\, we proposed that the\nrecruitment of a single Variant Surface G
 lycoprotein Expression Site (VSG-ES) telomeric locus to a discrete\, RNA p
 ol I-containing nuclear Body (ESB) defines\nthe mechanism responsible for 
 VSG mono-allelic expression. \n\nThe aim of the research in our group is t
 o identify the molecular mechanisms involved in nuclear body coherence and
  stability. Over the last few years we have searched for molecules involve
 d in ESB nuclear body regulation and have identified two classes of post-t
 ranslational protein modifications related to ESB stability and coherency.
  These modifications include the Small\nUbiquitin-like Modifier (SUMO) and
  protein phosphorylation. Importantly\, we have identified two proteins re
 sponsible for these modifications: the SP-RING SUMO ligase we named SIZ1 a
 nd the protein kinase TOR family.\n
LOCATION:Seminar Room\, Department of Pathology
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