BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Memento EPFL//
BEGIN:VEVENT
SUMMARY:Chemical approaches to decoding histone epigenetics
DTSTART:20230926T161500
DTEND:20230926T173000
DTSTAMP:20260414T211912Z
UID:0da9fc6a99f941b524652ca57989fdeb8c4c05b970449728b51a2bb7
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. David Li\, University of Honkg Kong\nHistone posttransla
 tional modifications (PTMs)\, such as phosphorylation\, methylation and ac
 etylation\, play crucial roles in regulating many fundamental cellular pro
 cesses\, such as gene transcription\, DNA replication\, DNA damage repair\
 , chromosome segregation and cell differentiation. Increasing evidences ha
 ve indicated that PTMs of histones can serve as a heritable ‘code’ (so
 -called ‘histone code’)\, which provides epigenetic information that a
  mother cell can pass to its daughters. Histone code is ‘written’ or 
 ‘erased’ by enzymes that generate or remove the modifications of histo
 nes. Meanwhile\, ‘readers’ of histone code recognize specific histone 
 modifications and ‘translate’ the code by executing distinct cellular 
 programs necessary to establish the diverse cell phenotypes.\n\nWhile a la
 rge number of PTMs have been identified on histones\, the biological signi
 ficance of vast majority of them remains poorly understood. This is partic
 ularly the case for those newly discovered histone modifications such as l
 ysine crotonylation\, succinylation\, fatty-acid acylation\, and the modif
 ications present at histone cores such as methylation at H3 lysine 79. Stu
 dies of these new PTMs are hindered by the lack of knowledge about their r
 egulating enzymes (i.e.\, ‘writers’ and ‘erasers’) and functional 
 binding proteins (i.e.\, ‘readers’). To fill this knowledge gap\, here
  I present the development of novel chemical tools and approaches\, in com
 bination with the state-of-the-art biochemistry\, proteomics and cell biol
 ogy methods\, to comprehensively identify ‘writers’\, ‘erasers’ an
 d ‘readers’ of histone PTMs and examine their regulatory mechanisms an
 d cellular functions.\n 
LOCATION:SV 1717 https://plan.epfl.ch/?room==SV%201717
STATUS:CONFIRMED
END:VEVENT
END:VCALENDAR
