BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Talks.cam//talks.cam.ac.uk//
X-WR-CALNAME:Talks.cam
BEGIN:VEVENT
SUMMARY:The Structural Basis of Ubiquitin Signalling - Cynthia Wolberger\,
  Johns Hopkins University
DTSTART:20110325T161500Z
DTEND:20110325T180000Z
UID:TALK30074@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:Ubiquitination is a reversible post-translational modification
  that regulates diverse processes in eukaryotic cells\, including protein 
 degradation\, transcription\, intracellular trafficking\, and the DNA dama
 ge response. The 76-amino acid ubiquitin protein is covalently attached to
  lysine side chains via its C-terminus\, and ubiquitin itself can be ubiqu
 itinated to give rise to a polyubiquitin chain. The precise nature of the 
 ubiquitin modification – monoubiquitin or polyubiquitin\, the particular
  lysine used to build up a polyubiquitin chain – governs the biological 
 consequence of the modification. I will describe structural and biochemica
 l studies of enzymes responsible for both ubiquitination and deubiquitinat
 ion\, as well as of the different nature of different types of polyubiquit
 in chains. I will present recent results on the four-protein DUB module of
  the SAGA complex\, which deubiquitinates histone H2B and plays a role in 
 transcription activation and elongation. The structure of the DUB complex 
 provides insights into how the different subunits activate the enzymatic a
 ctivity of the complex and target it to nucleosomal substrates. I will als
 o present studies of the SUMO-dependent E3 ligase\, RNF4\, and how the way
  in which it binds to ubiquitin-conjugating E2 enzymes governs the switch 
 between mono- and polyubiquitination. 
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
END:VEVENT
END:VCALENDAR