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PMID: 670187 Published · ppublish English Journal Article

Folding of 140-base pair length DNA by a core of arginine-rich histones.

The Journal of biological chemistry ·Vol. 253 ·No. 14 ·1978-07-25 ·Pages 5213-9

Bina-Stein M

Abstract

The nucleoprotein complex obtained by reconstitution of arginine-rich histones with 140-base pair length DNA has properties considerably closer to native core particles than the complex obtained with lysine-rich histones. A tetramer of arginine-rich histones folds 140-base pair length DNA into a particle (R body) with identical projections, on high resolution electron micrographs, as native core particles. The R body is more spherical in shape than the native nucleosome core particle. Both arginine- and lysine-rich histones contribute to the altered thermal stability and circular dichroism spectra of the core particle DNA.

MeSH Terms
Animals Arginine Chickens Circular Dichroism Deoxyribonucleoproteins Erythrocytes Histones Kinetics Microscopy, Electron Nucleic Acid Conformation Nucleic Acid Denaturation Nucleoproteins Protein Conformation
Chemicals
Deoxyribonucleoproteins Histones Nucleoproteins Arginine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Bina-Stein M
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1978-07-25
Pages
5213-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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