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SUMMARY:Peptide‐based probes for lysine deacetylases
DTSTART:20170920T150000
DTEND:20170920T163000
DTSTAMP:20260414T171504Z
UID:6836055b41f964a8a3c82707937a0cdb67bb8bb12b512c851fd4168e
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Dirk Schwarzer\, Universität Tübingen\nHistone deacety
 lases (HDACs) erase acetylation marks of lysine residues in histones and n
 on-histone proteins and thereby modulate the function and activity of thes
 e proteins. Alterations in protein acetylation levels and HDAC activity ar
 e transformations that occur in a wide range of diseases including cancer.
  Consequently\, HDACs have been established as promising drug targets. Imp
 ortantly\, these enzymes do not operate as single proteins but constitute 
 the catalytic domains of large multi-subunit HDAC complexes that modulate 
 HDAC activity and specificity. Recombinant assembly of such HDAC complexes
  is very challenging and consequently there is only little information abo
 ut their biochemical activity. We have developed peptide-based HDAC probes
  contain hydroxamate amino acids of various lengths replace modified lysin
 e residues. The interaction profiles of the endogenous human HDACs were st
 udied with different sets of probes\, which showed how substrate recogniti
 on and composition of HDAC complexes is modulated by the sequence context 
 of the acetylation sites. We further demonstrated that the interaction pro
 files reflect the catalytic activity of respective HDACs. These results un
 derline the utility of the newly established peptide-probes for decipherin
 g activity\, substrate selectivity and composition of endogenous HDAC comp
 lexes\, which can hardly be achieved otherwise
LOCATION:BCH 2218 https://plan.epfl.ch/?room==BCH%202218
STATUS:CONFIRMED
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