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SUMMARY:Proteomic exploration of the scope\, dynamics\, and stoichiometry 
 of lysine acetylation - Prof. Chunaram Choudhary | University of Copenhage
 n 
DTSTART:20190410T140000Z
DTEND:20190410T150000Z
UID:TALK118624@talks.cam.ac.uk
CONTACT:Hannah Burns
DESCRIPTION:Lysine acetylation is a key regulatory posttranslational modif
 ication. Function of lysine acetylation is most extensively studied in the
  context of epigenetic regulation of gene transcription via acetylation of
  histones. Recent mass spectrometry (MS)-based proteomic studies have grea
 tly expanded our knowledge of this modification. Our laboratory is using M
 S-based quantitative proteomics to map the scope of acetylation in diverse
  organisms and to investigate its dynamic regulation in response to geneti
 c and environmental perturbations. Furthermore\, we developed novel proteo
 mic methods to accurately quantify stoichiometry of acetylation on a prote
 ome-wide scale. Our results show that acetylation can occur through both e
 nzymatic and non-enzymatic mechanisms and suggest an important function of
  sub-cellular compartmentalization in the evolution of acetylation signali
 ng in eukaryotes. I will discuss our recently published and ongoing effort
 s in understanding acetylation signaling.
LOCATION:Sackler Lecture Theatre (Level 7) Wellcome Trust/MRC Building\, C
 ambridge Biomedical Campus
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