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© Adeline Mallet
Nématodes Caenorhabditis elegans en microscopie électronique à balayage.
Event

Developmental and Stem Cell Biology Department seminar by Doctor Serena Sanulli, UCSF, Department of Biochemistry and Biophysics/ Department of Pharmaceutical Chemistry

Scientific Fields
Diseases
Organisms
Applications
Technique
Date
19
Nov 2018
Time
11:00:00
Institut Pasteur, 25 Rue du Docteur Roux, 75015 Paris, France
Address
Building: Metchnikoff (#67) Room: Salle Jules Bordet
Location
2018-11-19 11:00:00 2018-11-19 12:00:00 Europe/Paris Developmental and Stem Cell Biology Department seminar by Doctor Serena Sanulli, UCSF, Department of Biochemistry and Biophysics/ Department of Pharmaceutical Chemistry “HP1 couples disorganization of the histone core to chromatin compaction and droplet formation” Invited Speaker: Serena Sanulli Postdoctoral Research fellow in Prof. Geeta Narlikar Lab, Departement of Biochemistry and Biophysics, and Prof. John D. […] Institut Pasteur, 25 Rue du Docteur Roux, 75015 Paris, France Germano Cecere germano.cecere@pasteur.fr

About

“HP1 couples disorganization of the histone core to chromatin compaction and droplet formation”

Invited Speaker: Serena Sanulli

Postdoctoral Research fellow in Prof. Geeta Narlikar Lab, Departement of Biochemistry and Biophysics, and Prof. John D. Gross Lab, Department of Pharmaceutical Chemistry, University of California, San Francisco.

 

Abstract: The heterochromatin protein HP1 is proposed to enable chromatin condensation and liquid droplet formation. Yet, how HP1 action at the nucleosome level drives higher-order chromatin organization remains unclear. Using hydrogen-deuterium exchange, NMR, and crosslinking mass-spectrometry, we show that the S. pombe HP1 protein, Swi6, substantially increases the accessibility and dynamics of buried histone residues within a nucleosome. Restraining these dynamics via site-specific disulfide bonds impairs the ability of Swi6 to bind nucleosomes and to condense chromatin into phase-separated droplets. Our results uncover a counter-intuitive function of Swi6, namely exposing buried regions of the histone octamer to achieve chromatin compaction. We propose that such exposed regions participate in transient multivalent interactions to drive higher-order chromatin organization in heterochromatin. Histone core dynamics may more generally regulate higher-order chromatin assemblies in contexts beyond heterochromatin. 

 

 

Location

Building: Metchnikoff (#67)
Room: Salle Jules Bordet
Address: Institut Pasteur, 25 Rue du Docteur Roux, 75015 Paris, France