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SUMMARY:Decoding chromatin modification states using chemical biology and 
 proteomic approaches
DTSTART:20171212T151500
DTEND:20171212T170000
DTSTAMP:20260307T130645Z
UID:0a960003392fa9d6b578f5437e8a1e6403f919e748368747e890c775
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Till Bartke\,   Institute of Functional Epigenetics Hel
 mholtz Zentrum München\nDNA and histone modifications play central roles 
 in the control of gene expression and errors in their regulation are assoc
 iated with a multitude of diseases. These modifications form an epigenetic
  ‘code’ that stores information within chromatin. This information is 
 “read” by epigenetic effector molecules that recognise DNA and histone
  modifications through specialised binding domains in order to regulate ch
 romatin function and to orchestrate subsequent biological events such as t
 ranscription\, DNA replication or DNA repair. It has become apparent in re
 cent years that DNA and histone modifications do not act in isolation but 
 form combinatorial modification signatures that define the functional stat
 e of the underlying chromatin. Our research aims to unravel how epigenetic
  effectors can read DNA and histone modification patterns and how they rec
 ognise different chromatin modification states. Our goal is to decipher th
 e “epigenetic code” by identifying epigenetic reader molecules that ca
 n integrate information from multiple chromatin modifications and to under
 stand how these factors operate at the molecular level. For this we are ta
 king two complementary approaches. Firstly\, we are tackling this problem 
 via a large-scale systems level approach in which we combine chemical biol
 ogy\, proteomic and computational methods to identify new factors and comp
 lexes that mediate the functions of specific chromatin states (Bartke et a
 l. 2010\, Cell 143\, 470). In addition\, we are interested in understandin
 g the molecular details of how epigenetic effectors ‘read out’ chromat
 in and we use biochemical\, cell biological\, and genomic techniques to in
 vestigate how these proteins recognise nucleosomal histone and DNA modific
 ations and how this contributes to their function (e.g. Borgel et al. 2017
 \, NAR 45\, 1114). I will present the latest results of our investigation 
 of the E3 ubiquitin ligase UHRF1\, a replication factor that reads meCpG- 
 and H3K9me3 modifications\, and our progress with SILAC Nucleosome Affinit
 y Purifications (SNAP) to decode chromatin.\n 
LOCATION:BCH 5310 https://plan.epfl.ch/?room==BCH%205310
STATUS:CONFIRMED
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