Histone core modifications regulating nucleosome structure and dynamics

2014 ◽  
Vol 15 (11) ◽  
pp. 703-708 ◽  
Author(s):  
Peter Tessarz ◽  
Tony Kouzarides
Keyword(s):  
Structure And Dynamics ◽  
Nucleosome Structure ◽  
Histone Core

Histone dynamics within the nucleosome play a critical role in SNF2h-mediated nucleosome sliding

2020 ◽  
Author(s):  
Nathan Gamarra ◽  
Geeta J. Narlikar
Keyword(s):  
Essential Feature ◽  
Critical Role ◽  
Protein Residues ◽  
Histone Octamer ◽  
Nucleosome Dynamics ◽  
Nucleosome Structure ◽  
Cryo Electron Microscopy ◽  
Disulfide Linkages ◽  
Nucleosome Sliding ◽  
Histone Core

AbstractElucidating the mechanisms by which ATP-dependent chromatin remodeling enzymes disrupt nucleosome structure is essential to understanding how chromatin states are established and maintained. A key finding informing remodeler mechanism is the observation that the dynamics of protein residues buried within the histone core of the nucleosome are used by specific remodelers to mobilize the nucleosome1. Recently, a study obtaining cryo-electron microscopy (cryo-EM) structures of ISWI-family remodelernucleosome complexes failed to observe stable conformational rearrangements in the histone octamer2. The authors of this study also failed to replicate the earlier finding that site-specifically restraining histone dynamics inhibits nucleosome sliding by ISWI-family remodelers1,2. In contrast, a recent cryo-EM structure detected asymmetric histone dynamics in an ISWI-nucleosome complex3. Here, using two different protocols, we replicate the original finding in Sinha et al.1 that dynamics within the histone core are important for nucleosome sliding by the human ISWI remodeler, SNF2h. These results firmly establish histone dynamics as an essential feature of ISWI-mediated nucleosome sliding and highlight the care required in designing and performing biochemical experiments investigating nucleosome dynamics using disulfide linkages.

Nucleosome Structure and Dynamics The DNA Minicircle Approach

2003 ◽  
pp. 79-102
Author(s):  
Ariel Prunell ◽  
Mohamed Alilat ◽  
Filomena De Lucia
Keyword(s):  
Structure And Dynamics ◽  
Nucleosome Structure

scholarly journals Impact of the Nucleosome Histone Core on the Structure and Dynamics of DNA-Containing Pyrimidine–Pyrimidone (6–4) Photoproduct

2020 ◽  
Vol 16 (9) ◽  
pp. 5972-5981
Author(s):  
Eva Matoušková ◽  
Emmanuelle Bignon ◽  
Victor E. P. Claerbout ◽  
Tomáš Dršata ◽  
Natacha Gillet ◽  
...  
Keyword(s):  
Structure And Dynamics ◽  
Histone Core

Structure and dynamics of the yeast SWR1-nucleosome complex

Science ◽  
2018 ◽  
Vol 362 (6411) ◽  
pp. eaat7716 ◽  
Author(s):  
Oliver Willhoft ◽  
Mohamed Ghoneim ◽  
Chia-Liang Lin ◽  
Eugene Y. D. Chua ◽  
Martin Wilkinson ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Adenosine Triphosphate ◽  
Single Molecule ◽  
Conformational Changes ◽  
Base Pair ◽  
Histone H2a ◽  
Substrate Interactions ◽  
Structure And Dynamics ◽  
Cryo Electron Microscopy ◽  
Histone Core

The yeast SWR1 complex exchanges histone H2A in nucleosomes with Htz1 (H2A.Z in humans). The cryo–electron microscopy structure of the SWR1 complex bound to a nucleosome at 3.6-angstrom resolution reveals details of the intricate interactions between components of the SWR1 complex and its nucleosome substrate. Interactions between the Swr1 motor domains and the DNA wrap at superhelical location 2 distort the DNA, causing a bulge with concomitant translocation of the DNA by one base pair, coupled to conformational changes of the histone core. Furthermore, partial unwrapping of the DNA from the histone core takes place upon binding of nucleosomes to SWR1 complex. The unwrapping, as monitored by single-molecule data, is stabilized and has its dynamics altered by adenosine triphosphate binding but does not require hydrolysis.

scholarly journals Consequences of Cisplatin Binding on Nucleosome Structure and Dynamics

2010 ◽  
Vol 17 (12) ◽  
pp. 1334-1343 ◽  
Author(s):  
Ryan C. Todd ◽  
Stephen J. Lippard
Keyword(s):  
Structure And Dynamics ◽  
Nucleosome Structure

scholarly journals Phosphorylation of Histone H3 Thr-45 Is Linked to Apoptosis

2009 ◽  
Vol 284 (24) ◽  
pp. 16575-16583 ◽  
Author(s):  
Paul J. Hurd ◽  
Andrew J. Bannister ◽  
Karen Halls ◽  
Mark A. Dawson ◽  
Michiel Vermeulen ◽  
...  
Keyword(s):  
Histone H3 ◽  
Histone Tails ◽  
Post Translational Modifications ◽  
Nucleosome Structure ◽  
Cytokine Inhibition ◽  
Dna Nicking ◽  
A Site ◽  
Histone Core

Numerous post-translational modifications have been identified in histones. Most of these occur within the histone tails, but a few have been identified within the histone core sequences. Histone core post-translational modifications have the potential to directly modulate nucleosome structure and consequently DNA accessibility. Here, we identify threonine 45 of histone H3 (H3T45) as a site of phosphorylation in vivo. We find that phosphorylation of H3T45 (H3T45ph) increases dramatically in apoptotic cells, around the time of DNA nicking. To further explore this connection, we analyzed human neutrophil cells because they are short-lived cells that undergo apoptosis in vivo. Freshly isolated neutrophils contain very little H3T45ph, whereas cells cultured for 20 h possess significant amounts; the kinetics of H3T45ph induction closely parallel those of caspase-3 activation. Cytokine inhibition of neutrophil apoptosis leads to reduced levels of H3T45ph. We identify protein kinase C-δ as the kinase responsible for H3T45ph in vitro and in vivo. Given the nucleosomal position of H3T45, we postulate that H3T45ph induces structural change within the nucleosome to facilitate DNA nicking and/or fragmentation.

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