Literature DB >> 1753964

[Structure of nucleosomes. Localization of the H2A and H2B histone segments interacting with DNA using DNA-protein crosslinking].

D Iu Gushchin, K K Ebralidze, A D Mirzabekov.   

Abstract

Histones' H2A and H2B peptidic points which interact with nucleosomal DNA have been identified by using the methods of DNA--protein covalent cross-linking. H2B can be linked to DNA via its N-terminal tail and via several lysines contained within residues 24-34. The most prominent site of histone H2A covalent linking to DNA is His-123, the less prominent being Lys-119 and Lys-124.

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Year:  1991        PMID: 1753964

Source DB:  PubMed          Journal:  Mol Biol (Mosk)        ISSN: 0026-8984


  3 in total

1.  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

2.  Nucleosomal structure at hyperacetylated loci probed in nuclei by DNA-histone crosslinking.

Authors:  K K Ebralidse; T R Hebbes; A L Clayton; A W Thorne; C Crane-Robinson
Journal:  Nucleic Acids Res       Date:  1993-10-11       Impact factor: 16.971

3.  Contacts of the globular domain of histone H5 and core histones with DNA in a "chromatosome".

Authors:  J J Hayes; D Pruss; A P Wolffe
Journal:  Proc Natl Acad Sci U S A       Date:  1994-08-02       Impact factor: 11.205

  3 in total

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