The structure of histone H1 and its location in chromatin

J. Allan; P. G. Hartman; C. Crane-robinson; F. X. Aviles

doi:10.1038/288675a0

The structure of histone H1 and its location in chromatin

J. Allan, P. G. Hartman, C. Crane-robinson, F. X. Aviles

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On the basis of their primary structure, the lysine-rich histones are a unified family of proteins. Each has an amino acid chain which falls into three distinct domains. Only the central domain (∼80 residues) is in a folded conformation. It is protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation. Without the flanking domains it is able to close two full turns of DNA in the nucleosome and can thus locate the H1 molecule. © 1980 Nature Publishing Group.

Idioma original	Anglès
Pàgines (de-a)	675-679
Revista	Nature
Volum	288
Número	5792
DOIs	https://doi.org/10.1038/288675a0
Estat de la publicació	Publicada - 1 de des. 1980

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10.1038/288675a0

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title = "The structure of histone H1 and its location in chromatin",

abstract = "On the basis of their primary structure, the lysine-rich histones are a unified family of proteins. Each has an amino acid chain which falls into three distinct domains. Only the central domain (∼80 residues) is in a folded conformation. It is protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation. Without the flanking domains it is able to close two full turns of DNA in the nucleosome and can thus locate the H1 molecule. {\textcopyright} 1980 Nature Publishing Group.",

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T1 - The structure of histone H1 and its location in chromatin

AU - Allan, J.

AU - Hartman, P. G.

AU - Crane-robinson, C.

AU - Aviles, F. X.

PY - 1980/12/1

Y1 - 1980/12/1

N2 - On the basis of their primary structure, the lysine-rich histones are a unified family of proteins. Each has an amino acid chain which falls into three distinct domains. Only the central domain (∼80 residues) is in a folded conformation. It is protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation. Without the flanking domains it is able to close two full turns of DNA in the nucleosome and can thus locate the H1 molecule. © 1980 Nature Publishing Group.

AB - On the basis of their primary structure, the lysine-rich histones are a unified family of proteins. Each has an amino acid chain which falls into three distinct domains. Only the central domain (∼80 residues) is in a folded conformation. It is protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation. Without the flanking domains it is able to close two full turns of DNA in the nucleosome and can thus locate the H1 molecule. © 1980 Nature Publishing Group.

U2 - 10.1038/288675a0

DO - 10.1038/288675a0

M3 - Article

SN - 0028-0836

VL - 288

SP - 675

EP - 679

JO - Nature

JF - Nature

IS - 5792

ER -

The structure of histone H1 and its location in chromatin

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