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Tuesday, October 23rd, 2018
Centre de Recherche - Paris - Amphithéâtre Antoine Lacassagne

Structural and functional diversity in ATP-dependent nucleosome remodelers

ATP-dependent nucleosome remodeling factors (“remodelers”) use the energy from ATP hydrolysis to non-covalently modify the structure of nucleosomes, the basic unit of DNA packaging in eukaryotic genomes. Remodelers are conserved from yeast to humans, and while they are very diverse in composition--ranging from single-subunit remodelers to multi-subunit complexes of > 1MDa--they all contain a conserved core ATPase that uses DNA translocation to break histone-DNA contacts. Despite this common core, remodelers are capable of producing very different outcomes, from sliding a histone octamer along the DNA, to ejecting histone dimers or octamers, to swapping histone dimers for variant forms.

We are interested in understanding the mechanisms underlying this functional versatility. I will present structural (cryo-EM) and functional data on two different systems: (1) A minimal version of the RSC remodeling complex (a member of the SWI/SNF family of remodelers), which can both slide and eject histone octamers; and (2) CSB, a so-called “orphan” remodeler that plays a role in Transcription-Coupled DNA repair. We recently showed that CSB uses its DNA translocation activity to function as a processivity factor for RNA Polymerase II.

Event poster


Andres Leschziner

Department of Cellular and Molecular Medicine and Division of Biological Sciences, University of California San Diego La Jolla, CA, USA

Hosted by

Invited by

Domain 2 - UMR 3215 / U934 - Genetics and Developmental Biology

Institut Curie

Manuel THERY
Hôpital Saint Louis, Paris

CytoMorpho Lab, LPCV / BIG / DRF / CEA


Manuel THERY

CytoMorpho Lab, LPCV / BIG / DRF / CEA

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