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PMID: 896477 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Conformational states of chromatin nu bodies induced by urea.

Nucleic acids research ·Vol. 4 ·No. 6 ·1977-06-00 ·Pages 1911-31

Olins DE, Bryan PN, Harrington RE, Hill WE, Olins AL

Abstract

Monomer chromatin nu bodies (nu1) from chicken erythrocyte nuclei were exposed to 0-10 M urea plus 0.2 mM EDTA (PH 7). Alterations in nu1 conformation were examined using hydrodynamic methods (i.e., S, eta, and (formula: see text)), thermal denaturation, circular dichroism, reactivity of histone thiol groups to N-ethyl maleimide, and electron microscopy. The two domains of a nu body (i.e., the DNA-rich shell and the protein-rich core) aeared to respond differently to the destabilizing effects of increasing urea; DNA conformation and stability exhibited noncooperative changes; the core protein structure revealed cooperative destabilization between 4 and 7 M urea. Companion studies on the conformation of the inner histone "heterotypic tetramer" also revealed cooperative destabilization with increasing urea concentration.

MeSH Terms
Animals Chickens Chromatin Circular Dichroism DNA Erythrocytes Ethylmaleimide Histones Hot Temperature Microscopy, Electron Nucleic Acid Conformation/drug effects Nucleic Acid Denaturation Urea/pharmacology
Chemicals
Chromatin Histones Urea DNA Ethylmaleimide
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Olins D E
Bryan P N
Harrington R E
Hill W E
Olins A L
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37 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/4.6.1911
Published
1977-06-00
Pages
1911-31
Language
English
Region
England
NLM ID
0411011
PMCID
PMC342531
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/4.6.1911 PMC Full Text View journal details
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