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The N tails of histones H3 and H4 adopt a highly structured conformation in the nucleosome.

Abstract：

:The histone N tails correspond to conserved amino acid sequences that are peripherally located in the nucleosome and undergo a variety of post-synthetic modifications during cell cycle. These N tails have been recently recognized as directly interacting with transcription-related proteins. We show here, based on circular dichroic evidence, that the N tails of both tetrameric histones H3 and H4 are highly organized as DNA-bound polypeptide segments in the nucleosome core particle, with about half of their residues, taken together, being alpha-helical. In contrast, the N tails of both dimeric histones H2A and H2B are found essentially in a random-coil conformation. The implications of these findings on nucleosome structure and recognition are discussed.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Banères JL,Martin A,Parello J

doi

10.1006/jmbi.1997.1297

subject

Has Abstract

pub_date

1997-10-31 00:00:00

pages

503-8

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(97)91297-3

journal_volume

273

pub_type

杂志文章

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