scholarly journals The Divalent Cations Ca2+and Mg2+Play Specific Roles in Stabilizing Histone–DNA Interactions within Nucleosomes That Are Partially Redundant with the Core Histone Tail Domains

Biochemistry ◽  
2011 ◽  
Vol 50 (46) ◽  
pp. 9973-9981 ◽  
Author(s):  
Zungyoon Yang ◽  
Jeffrey J. Hayes
Keyword(s):  
Divalent Cations ◽  
Core Histone ◽  
Dna Interactions ◽  
Histone Tail ◽  
The Core ◽  
Core Histone Tail

scholarly journals Preferential interaction of the core histone tail domains with linker DNA

2001 ◽  
Vol 98 (12) ◽  
pp. 6599-6604 ◽  
Author(s):  
D. Angelov ◽  
J. M. Vitolo ◽  
V. Mutskov ◽  
S. Dimitrov ◽  
J. J. Hayes
Keyword(s):  
Core Histone ◽  
Histone Tail ◽  
Preferential Interaction ◽  
The Core ◽  
Core Histone Tail

Physical methods used to study core histone tail structures and interactions in solutionThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process.

2006 ◽  
Vol 84 (4) ◽  
pp. 578-588 ◽  
Author(s):  
Xiaodong Wang ◽  
Jeffrey J. Hayes
Keyword(s):  
Peer Review Process ◽  
Regulatory Elements ◽  
Core Histone ◽  
Histone Tail ◽  
Tertiary Structures ◽  
Post Translational Modifications ◽  
Binding Behavior ◽  
The Core ◽  
Solution Methods ◽  
Core Histone Tail

The core histone tail domains are key regulatory elements in chromatin. The tails are essential for folding oligonucleosomal arrays into both secondary and tertiary structures, and post-translational modifications within these domains can directly alter DNA accessibility. Unfortunately, there is little understanding of the structures and interactions of the core histone tail domains or how post-translational modifications within the tails may alter these interactions. Here we review NMR, thermal denaturation, cross-linking, and other selected solution methods used to define the general structures and binding behavior of the tail domains in various chromatin environments. All of these methods indicate that the tail domains bind primarily electrostatically to sites within chromatin. The data also indicate that the tails adopt specific structures when bound to DNA and that tail structures and interactions are plastic, depending on the specific chromatin environment. In addition, post-translational modifications, such as acetylation, can directly alter histone tail structures and interactions.

scholarly journals Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure

Chromosoma ◽  
2013 ◽  
Vol 123 (1-2) ◽  
pp. 3-13 ◽  
Author(s):  
Sharon Pepenella ◽  
Kevin J. Murphy ◽  
Jeffrey J. Hayes
Keyword(s):  
Chromatin Structure ◽  
Higher Order ◽  
Core Histone ◽  
Histone Tail ◽  
The Core ◽  
Core Histone Tail

scholarly journals Short and long range Inter‐nucleosome interactions of the core histone tail domains

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Jeffrey Hayes ◽  
Pu‐Yeh Kan ◽  
Xiaodong Wang ◽  
Xu Lu ◽  
Jeffrey Hansen
Keyword(s):  
Long Range ◽  
Core Histone ◽  
Histone Tail ◽  
The Core ◽  
Core Histone Tail

Structures and interactions of the core histone tail domains

Biopolymers ◽  
2003 ◽  
Vol 68 (4) ◽  
pp. 539-546 ◽  
Author(s):  
Chunyang Zheng ◽  
Jeffrey J. Hayes
Keyword(s):  
Core Histone ◽  
Histone Tail ◽  
The Core ◽  
Core Histone Tail

Reversible Oligonucleosome Self-Association:  Dependence on Divalent Cations and Core Histone Tail Domains†

Biochemistry ◽  
1996 ◽  
Vol 35 (13) ◽  
pp. 4009-4015 ◽  
Author(s):  
Patricia M. Schwarz ◽  
Alicia Felthauser ◽  
Terace M. Fletcher ◽  
Jeffrey C. Hansen
Keyword(s):  
Divalent Cations ◽  
Core Histone ◽  
Histone Tail ◽  
Self Association ◽  
Core Histone Tail

scholarly journals The Core Histone N-Terminal Tail Domains Negatively Regulate Binding of Transcription Factor IIIA to a Nucleosome Containing a 5S RNA Gene via a Novel Mechanism

2005 ◽  
Vol 25 (1) ◽  
pp. 241-249 ◽  
Author(s):  
Zungyoon Yang ◽  
Chunyang Zheng ◽  
Christophe Thiriet ◽  
Jeffrey J. Hayes
Keyword(s):  
Transcription Factor ◽  
Transcription Activation ◽  
Core Histone ◽  
Histone Tail ◽  
Binding Studies ◽  
5S Rna ◽  
Activation Domain ◽  
The Core ◽  
Transcription Activation Domain ◽  
Core Histone Tail

ABSTRACT Reconstitution of a DNA fragment containing a 5S RNA gene from Xenopus borealis into a nucleosome greatly restricts binding of the primary 5S transcription factor, TFIIIA. Consistent with transcription experiments using reconstituted templates, removal of the histone tail domains stimulates TFIIIA binding to the 5S nucleosome greater than 100-fold. However, we show that tail removal increases the probability of 5S DNA unwrapping from the core histone surface by only approximately fivefold. Moreover, using site-specific histone-to-DNA cross-linking, we show that TFIIIA binding neither induces nor requires nucleosome movement. Binding studies with COOH-terminal deletion mutants of TFIIIA and 5S nucleosomes reconstituted with native and tailless core histones indicate that the core histone tail domains play a direct role in restricting the binding of TFIIIA. Deletion of only the COOH-terminal transcription activation domain dramatically stimulates TFIIIA binding to the native nucleosome, while further C-terminal deletions or removal of the tail domains does not lead to further increases in TFIIIA binding. We conclude that the unmodified core histone tail domains directly negatively influence TFIIIA binding to the nucleosome in a manner that requires the C-terminal transcription activation domain of TFIIIA. Our data suggest an additional mechanism by which the core histone tail domains regulate the binding of trans-acting factors in chromatin.

scholarly journals The Core Histone Tail Domains Contribute to Sequence-dependent Nucleosome Positioning

2007 ◽  
Vol 282 (11) ◽  
pp. 7930-7938 ◽  
Author(s):  
Zungyoon Yang ◽  
Chunyang Zheng ◽  
Jeffrey J. Hayes
Keyword(s):  
Nucleosome Positioning ◽  
Core Histone ◽  
Histone Tail ◽  
The Core ◽  
Sequence Dependent ◽  
Core Histone Tail
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