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SUMMARY: Allostery and intrinsic disorder mediate transcription regulation
  by conditional cooperativity -  Abel Garcia-Pino\,University of Brussels\
 , Belgium
DTSTART:20110408T000000Z
DTEND:20110408T010000Z
UID:TALK30704@talks.cam.ac.uk
CONTACT:benedetta bolognesi
DESCRIPTION:Toxin-antitoxin (TA) modules are small stress response operons
  encoding a toxin that targets transcription and/or translation and a corr
 esponding neutralizing antitoxin. They are involved in the stabilization o
 f low copy number plasmids and may play a role in the stress physiology of
  bacteria. While the relevance and cellular actions of TA modules are beco
 ming clear\, the regulation at the molecular level remains a challenging t
 opic. The regulation of toxin-antitoxin operons usually involves the toxin
  acting as co- or de-repressor depending on the ratio toxin/antitoxin. Thi
 s unexplained transcriptional regulatory phenomenon is known as conditiona
 l cooperativity. Using the phd/doc operon as model system\, we have found 
 that binding of the toxin Doc to the C-terminal intrinsically disordered s
 egment of Phd\, induces order in the N-terminal DNA binding domain of Phd(
 1). Based on substantial structural and biophysical evidences we propose a
  model for the conditional cooperative regulation of transcription\, typic
 al of TA systems\, that involves allosteric coupling between two partially
  disordered domains\, which may be applicable for the regulation of other 
 biological systems.\n\n(1) Garcia-Pino A.\, Balasubramanian S.\, L.\, Ehud
  Gazit E.\, Magnuson R.D.\, Charlier D.\, Loris R.\, Transcriptional regul
 ation by conditional co-operativity mediated by allosteric coupling betwee
 n two disordered domains. (2010) Cell Jul 9\;142(1):101-11\n\n(2) De Jonge
  N\, Garcia-Pino A\, Buts L\, Haesaerts S\, Charlier D\, Zangger K\, Wyns 
 L\, De Greve H\, Loris R. Rejuvenation of CcdB-poisoned gyrase by an intri
 nsically disordered protein domain. Mol Cell. (2009) Jul 31\;35(2):154-6
LOCATION:Unilever Lecture Theatre\,  Department of Chemistry
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