Removal of histone tails from nucleosome dissects the physical mechanisms of salt-induced aggregation, linker histone H1-induced compaction, and 30-nm fiber formation of the nucleosome array

Ultramicroscopy

Volumn 109, Issue 8, 2009, Pages 868-873

  Hizume, Kohji ^a   Nakai, Tonau ^b   Araki, Sumiko ^a   Prieto, Eloise ^a   Yoshikawa, Kenichi ^a   Takeyasu, Kunio ^a  

^a KYOTO UNIVERSITY   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

Author keywords

Atomic force microscopy; Chromatin; Electron microscopy; Histone tail; Nucleosome; Scanning tunneling and atomic force microscopy

Indexed keywords

CHROMATIN; CHROMATIN FIBERS; CHROMATIN STRUCTURE; FIBER FORMATION; HIGH SALT CONCENTRATION; HIGHER ORDER; HISTONE TAIL; IN-VITRO; LINKER HISTONES; N-TERMINAL; NUCLEOSOMAL ARRAYS; NUCLEOSOME; NUCLEOSOME ARRAYS; NUCLEOSOMES; PHYSICAL MECHANISM; SALT-INDUCED AGGREGATION; SCANNING TUNNELING AND ATOMIC FORCE MICROSCOPY;

ATOMIC FORCE MICROSCOPY; ATOMS; NUCLEIC ACIDS; SALT REMOVAL; SCANNING;

CHROMOSOMES;

HISTONE H1;

AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CHROMATIN; CHROMATIN STRUCTURE; CONTROLLED STUDY; DNA TEMPLATE; HUMAN; HUMAN CELL; IN VITRO STUDY; MOLECULAR INTERACTION; NUCLEOSOME;

HISTONES; MACROMOLECULAR SUBSTANCES; MICROSCOPY, ATOMIC FORCE; NUCLEOSOMES; PLASMIDS; PROTEIN BINDING; SALTS;

EID: 67449158760     PISSN: 03043991     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ultramic.2009.03.014     Document Type: Article

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