Literature DB >> 6509040

Differential dissociation of histone tails from core chromatin.

I O Walker.   

Abstract

The dissociation of the trypsin-sensitive basic tails of the core histones in core chromatin has been followed as a function of [NaCl] using proton NMR spectroscopy. The tails dissociate in a highly cooperative all or none manner over the salt concentration range 0.2-0.6 M, that is, below the salt concentration required to dissociate the complete molecule. Assuming that each basic tail dissociates independently, the total number of salt linkages involved in binding the tails to DNA is 103. This equals the number of basic side chains in the tails of an octamer. The standard free energy of dissociation, delta G degree, in 1 M NaCl at 297 K is 3.6 kcal/mol. Temperature had no effect on the extent of dissociation up to 45 degrees C. However, between 45 and 65 degrees C, where the premelting transition in the core chromatin occurs, the tails dissociated completely. Dissociation of the tails was associated with a conformational transition in the DNA consistent with loss of supercoiling. From this, and the results of a previous study, it can be shown that the structured, trypsin-resistant domain of each core histone octamer makes 100 salt linkages to DNA. Thus, in 10 mM salt, each core octamer makes a total of 203 salt linkages to DNA.

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Year:  1984        PMID: 6509040     DOI: 10.1021/bi00318a037

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  17 in total

Review 1.  Chromatin modification and disease.

Authors:  C A Johnson
Journal:  J Med Genet       Date:  2000-12       Impact factor: 6.318

2.  Preferential interaction of the core histone tail domains with linker DNA.

Authors:  D Angelov; J M Vitolo; V Mutskov; S Dimitrov; J J Hayes
Journal:  Proc Natl Acad Sci U S A       Date:  2001-05-29       Impact factor: 11.205

Review 3.  Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure.

Authors:  Sharon Pepenella; Kevin J Murphy; Jeffrey J Hayes
Journal:  Chromosoma       Date:  2013-08-31       Impact factor: 4.316

4.  Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.

Authors:  Hongbo Xie; Slobodan Vucetic; Lilia M Iakoucheva; Christopher J Oldfield; A Keith Dunker; Vladimir N Uversky; Zoran Obradovic
Journal:  J Proteome Res       Date:  2007-03-29       Impact factor: 4.466

5.  Salt-induced conformation and interaction changes of nucleosome core particles.

Authors:  Stéphanie Mangenot; Amélie Leforestier; Patrice Vachette; Dominique Durand; Françoise Livolant
Journal:  Biophys J       Date:  2002-01       Impact factor: 4.033

6.  Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding.

Authors:  V Mutskov; D Gerber; D Angelov; J Ausio; J Workman; S Dimitrov
Journal:  Mol Cell Biol       Date:  1998-11       Impact factor: 4.272

7.  Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin.

Authors:  K P Nightingale; R E Wellinger; J M Sogo; P B Becker
Journal:  EMBO J       Date:  1998-05-15       Impact factor: 11.598

8.  The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core.

Authors:  K M Lee; J J Hayes
Journal:  Proc Natl Acad Sci U S A       Date:  1997-08-19       Impact factor: 11.205

9.  Laser-induced crosslinking of histones to DNA in chromatin and core particles: implications in studying histone-DNA interactions.

Authors:  S I Dimitrov; V R Russanova; D Angelov; I G Pashev
Journal:  Nucleic Acids Res       Date:  1989-12-11       Impact factor: 16.971

10.  A universal description for the experimental behavior of salt-(in)dependent oligocation-induced DNA condensation.

Authors:  Nikolay Korolev; Nikolay V Berezhnoy; Khee Dong Eom; James P Tam; Lars Nordenskiöld
Journal:  Nucleic Acids Res       Date:  2009-11       Impact factor: 16.971

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