Literature DB >> 3712436

Salt-dependent co-operative interaction of histone H1 with linear DNA.

D J Clark, J O Thomas.   

Abstract

The nature of the complexes formed between histone H1 and linear double-stranded DNA is dependent on ionic strength and on the H1 : DNA ratio. At an input ratio of less than about 60% (w/w) H1 : DNA, there is a sharp transition from non-co-operative to co-operative binding at a critical salt concentration that depends on the DNA size and is in the range 20 to 50 mM-NaCl. Above this critical ionic strength the H1 binds to only some of the DNA molecules leaving the rest free, as shown by sedimentation analysis. The ionic strength range over which this change in behaviour occurs is also that over which chromatin folding is induced. Above the salt concentration required for co-operative binding of H1 to DNA, but not below it, H1 molecules are in close proximity as shown by the formation of H1 polymers upon chemical cross-linking. The change in binding mode is not driven by the folding of the globular domain of H1, since this is already folded at low salt in the presence of DNA, as indicated by its resistance to tryptic digestion. The H1-DNA complexes at low salt, where H1 is bound distributively to all DNA molecules, contain thickened regions about 6 nm across interspersed with free DNA, as shown by electron microscopy. The complexes formed at higher salt through co-operative interactions are rods of relatively uniform width (11 to 15 nm) whose length is about 1.6 times shorter than that of the input DNA, or are circular if the DNA is long enough. They contain approximately 70% (w/w) H1 : DNA and several DNA molecules. These thick complexes can also be formed at low salt (15 mM-NaCl) when the H1 : DNA input ratio is sufficiently high (approximately 70%).

Entities:  

Mesh:

Substances:

Year:  1986        PMID: 3712436     DOI: 10.1016/0022-2836(86)90335-9

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  44 in total

1.  Structure of transfection-active histone H1/DNA complexes.

Authors:  H Lucius; A Haberland; S Zaitsev; R Dallüge; M Schneider; M Böttger
Journal:  Mol Biol Rep       Date:  2001       Impact factor: 2.316

2.  Structure analysis of purified histone H5 and of H5 in nuclei by limited proteolysis.

Authors:  M Hallupp; F Buck; W H Strätling
Journal:  Biochem J       Date:  1992-03-01       Impact factor: 3.857

3.  Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome.

Authors:  Sajad Hussain Syed; Damien Goutte-Gattat; Nils Becker; Sam Meyer; Manu Shubhdarshan Shukla; Jeffrey J Hayes; Ralf Everaers; Dimitar Angelov; Jan Bednar; Stefan Dimitrov
Journal:  Proc Natl Acad Sci U S A       Date:  2010-05-10       Impact factor: 11.205

4.  Cooperative binding of the globular domains of histones H1 and H5 to DNA.

Authors:  J O Thomas; C Rees; J T Finch
Journal:  Nucleic Acids Res       Date:  1992-01-25       Impact factor: 16.971

5.  Structural appearance of linker histone H1/siRNA complexes.

Authors:  Annekathrin Haberland; Sergei Zaitsev; Norbert Waldöfner; Bettina Erdmann; Michael Böttger; Wolfgang Henke
Journal:  Mol Biol Rep       Date:  2008-06-20       Impact factor: 2.316

6.  Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure.

Authors:  Andrew Routh; Sara Sandin; Daniela Rhodes
Journal:  Proc Natl Acad Sci U S A       Date:  2008-06-26       Impact factor: 11.205

7.  Co-operative interactions of oligonucleosomal DNA with the H1e histone variant and its poly(ADP-ribosyl)ated isoform.

Authors:  M D'erme; G Zardo; A Reale; P Caiafa
Journal:  Biochem J       Date:  1996-06-01       Impact factor: 3.857

8.  Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain.

Authors:  Tamara L Caterino; He Fang; Jeffrey J Hayes
Journal:  Mol Cell Biol       Date:  2011-04-04       Impact factor: 4.272

9.  Identification of two DNA-binding sites on the globular domain of histone H5.

Authors:  F A Goytisolo; S E Gerchman; X Yu; C Rees; V Graziano; V Ramakrishnan; J O Thomas
Journal:  EMBO J       Date:  1996-07-01       Impact factor: 11.598

10.  Histone H1 preferentially binds to superhelical DNA molecules of higher compaction.

Authors:  M Ivanchenko; J Zlatanova; K van Holde
Journal:  Biophys J       Date:  1997-03       Impact factor: 4.033

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.