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SUMMARY:Single molecule analysis of p53 binding in living cells following 
 activation by DNA damage
DTSTART:20160519T100000
DTSTAMP:20260513T070542Z
UID:57dc0f63744dda41742a349a94ec8a26076c71be1e0d0f5a5cc6627e
CATEGORIES:Conferences - Seminars
DESCRIPTION:Dr. Davide Mazza\nCentro di Imaging Sperimentale\, San Raffael
 e Scientific Institute\,\nand the Università Vita-Salute San Raffaele\, M
 ilano\, Italy\nThe binding of transcription factors (TFs) to their regulat
 ory sites on DNA determines how much and how timely a particular gene will
  be expressed\, and ultimately how the cell respond to external cues. TF b
 inding is typically studied by bulk biochemical experiments as chromatin i
 mmunoprecipitation (ChIP). These methods has limited temporal resolution a
 nd typically requires a large number of cells to be pooled and analyzed to
 gether:  the interpretation of ChIP results can therefore be challenging 
 when dealing with TFs exhibiting rapid turnover\, or with cells and tissue
 s exhibiting a patterned non-homogeneous transcriptional response to an ex
 ternal stimulus.\nWe describe a microscopy-based single molecule imaging a
 pproach which can be used to obtain direct information on the TF binding k
 inetics to chromatin with the sub-second temporal resolution at the indivi
 dual live-cell level [1\,2]. We apply this method to characterize the bind
 ing of the tumor suppressor p53 both in basal\, non-stimulated conditions 
 and upon its activation by genotoxic stress induced by ionizing radiation:
  we show that p53 binds transiently to DNA (timescale of seconds)\, and th
 at this interaction is modulated following the induction of damage\, Impor
 tantly\, more stable interactions are associated to higher transcription r
 ates of a p53 target gene\, indicating that p53 acts as a latent TF\, revi
 ving an hypothesis initially derived from in-vitro studies [3]\, but later
  challenged by low temporal resolution ChIP experiments [4].\n[1] D. Mazza
  et al.\, Nucl. Ac. Res. 2012\, 40\, 119.\n[2] D. Mazza et al.\, Nat. Meth
 . 2013\, 10\, 691.\n[3] T. Yakovleva\, et al.\, Trends Biochem Sci. 2002\,
  27\, 612.\n[4] M.D. Kaeser\, R.D. Iggo. PNAS. 2002\, 99\, 95.
LOCATION:room 407\, 4th floor\, Cubotron/Unil
STATUS:CONFIRMED
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