Literature DB >> 1170889

Dynamic equilibrium in histone assembly: self-assembly of single histones and histone pairs.

R Sperling, M Bustin.   

Abstract

The assembly of acid-extracted, purified F2a1, F3, F2a2, and F2b histones and their six possible pairwise combination into organized structures has been studied by: (1) sedimentation velocity, (2) sedimentation equilibrium, (3) electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate after cross-linking the protein solution with dimethyl suberimidate, and (4) electron microscopy. Each of the purified histone fractions can renature and assemble into high molecular weight organized structures. This assembly is dependent on the ionic strength, protein concentration, and temperature of the solutions. The four histones studied assemble into structures of similar dimensions and shape. In each case the first structure observed is a bent rod with a diameter of 22 A. Conditions which favor assembly lead to formation of fibers with diameters of about 44 A. The conditions which lead to assembly into organized structures are similar for the arginine-rich histones, F2a1 and F3. Higher ionic strength is required for the assembly of the lysine-rich histones, F2a2 and F2b. Certain pairs of histones interact. Strong interactions among pairs of histones interfere with the self-assembly of single histones into large structures. Howver, increase in protein concentration or ionic stregth leads to formation of large molecular structures even in solutions of pairs of strongly interacting histones. These structures are similar to those obtained with single histones. The results suggest that aggregation and complexing of histones represent a reversible, ordered process of assembly. The various assembled forms are in a dynamic equilibrium. The final assembled form, which is similar in all cases, is dependent on the environmental conditions to which the histones are exposed. It is suggested that each of the assembled histone structures, regardless whether it is composed of a single histone or a pair of histones, can serve as a core around which the DNA can be wrapped.

Entities:  

Mesh:

Substances:

Year:  1975        PMID: 1170889     DOI: 10.1021/bi00686a006

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


  10 in total

1.  Some properties of tobacco protoplast chromatin.

Authors:  C Gigot; G Philipps; A Nicolaieff; L Hirth
Journal:  Nucleic Acids Res       Date:  1976-09       Impact factor: 16.971

2.  Histone dimers: a fundamental unit in histone assembly.

Authors:  R Sperling; M Bustin
Journal:  Nucleic Acids Res       Date:  1976-05       Impact factor: 16.971

3.  Arrangement of subunits in assembled histone H4 fibers.

Authors:  R Sperling; L A Amos
Journal:  Proc Natl Acad Sci U S A       Date:  1977-09       Impact factor: 11.205

4.  The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization.

Authors:  G Arents; E N Moudrianakis
Journal:  Proc Natl Acad Sci U S A       Date:  1995-11-21       Impact factor: 11.205

5.  Photochemical cross-linking of histones to DNA nucleosomes.

Authors:  J Sperling; R Sperling
Journal:  Nucleic Acids Res       Date:  1978-08       Impact factor: 16.971

6.  Low resolution models of self-assembled histone fibers from X-ray diffraction studies.

Authors:  E J Wachtel; R Sperling
Journal:  Nucleic Acids Res       Date:  1979-01       Impact factor: 16.971

7.  Infrared spectroscopy and X-ray diffraction study of complexes of histones H3 and H4 in the condensed state.

Authors:  E J Wachtel; C Gilon; R Sperling
Journal:  Nucleic Acids Res       Date:  1981-08-11       Impact factor: 16.971

8.  The helical model of the nucleosome core.

Authors:  E Trifonov
Journal:  Nucleic Acids Res       Date:  1978-04       Impact factor: 16.971

9.  Nucleosome core histone complex isolated gently and rapidly in 2 M NaCl is octameric.

Authors:  M Philip; M Jamaluddin; R V Sastry; H S Chandra
Journal:  Proc Natl Acad Sci U S A       Date:  1979-10       Impact factor: 11.205

10.  Histones have high affinity for the glomerular basement membrane. Relevance for immune complex formation in lupus nephritis.

Authors:  T M Schmiedeke; F W Stöckl; R Weber; Y Sugisaki; S R Batsford; A Vogt
Journal:  J Exp Med       Date:  1989-06-01       Impact factor: 14.307

  10 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.