Histone mark recognition controls nucleosome ...
Document type :
Article dans une revue scientifique
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Title :
Histone mark recognition controls nucleosome translocation via a kinetic proofreading mechanism: Confronting theory and high-throughput experiments
Author(s) :
Blossey, Ralf [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Schiessel, Helmut [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Schiessel, Helmut [Auteur]
Journal title :
Physical Review E
Abbreviated title :
Phys. Rev. E
Volume number :
99
Publisher :
American Physical Society (APS)
Publication date :
2019-06-10
HAL domain(s) :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Chromatin remodelers are multidomain enzymatic motor complexes that displace nucleosomes along DNA and hence “remodel chromatin structure,” i.e., they dynamically reorganize nucleosome positions in both gene activation and ...
Show more >Chromatin remodelers are multidomain enzymatic motor complexes that displace nucleosomes along DNA and hence “remodel chromatin structure,” i.e., they dynamically reorganize nucleosome positions in both gene activation and gene repression. Recently, experimental insights from structural biology methods and remodeling assays have substantially advanced the understanding of these key chromatin components. Here we confront the kinetic proofreading scenario of chromatin remodeling, which proposes a mechanical link between histone residue modifications and the ATP-dependent action of remodelers, with recent experiments. We show that recent high-throughput data on nucleosome libraries assayed with remodelers from the Imitation Switch family are in accord with our earlier predictions of the kinetic proofreading scenario. We make suggestions for experimentally verifiable predictions of the kinetic proofreading scenarios for remodelers from other families.Show less >
Show more >Chromatin remodelers are multidomain enzymatic motor complexes that displace nucleosomes along DNA and hence “remodel chromatin structure,” i.e., they dynamically reorganize nucleosome positions in both gene activation and gene repression. Recently, experimental insights from structural biology methods and remodeling assays have substantially advanced the understanding of these key chromatin components. Here we confront the kinetic proofreading scenario of chromatin remodeling, which proposes a mechanical link between histone residue modifications and the ATP-dependent action of remodelers, with recent experiments. We show that recent high-throughput data on nucleosome libraries assayed with remodelers from the Imitation Switch family are in accord with our earlier predictions of the kinetic proofreading scenario. We make suggestions for experimentally verifiable predictions of the kinetic proofreading scenarios for remodelers from other families.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
Computational Molecular Systems Biology
Submission date :
2021-01-04T10:30:10Z
2021-01-06T14:07:06Z
2021-01-06T14:07:06Z
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