Premium
DNA recognition and nucleosome organization
Author(s) -
Travers Andrew,
Drew Horace
Publication year - 1997
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1997)44:4<423::aid-bip6>3.0.co;2-m
Subject(s) - histone octamer , nucleosome , linker dna , chemistry , chromatosome , histone , chromatin , dna , biophysics , base pair , sequence (biology) , computational biology , crystallography , stereochemistry , biochemistry , biology
The affinity of a DNA sequence for the histone octamer in a core nucleosome depends on the intrinsic flexibility of the DNA. This parameter can be affected both by the sequence‐dependent conformational preferences of individual base steps and by the nature and location of the exocyclic groups of the DNA bases. By adopting highly preferred conformations particular types of base step can influence the rotational positioning of the DNA on the surface of the histone octamer. The asymmetry of the next higher order of chromatin structure is determined in part by the asymmetric binding of the globular domain of histone H5 to the core nucleosome. © 1998 John Wiley & Sons, Inc. Biopoly 44: 423–433 1997