The premelting of nucleoprotein: role of non-histone proteins

In native nucleoprotein, the premelting structural changes of DNA are not observed by circular dichroism measurements. In order to determine which protein fraction of chromatin is responsible for the absence of premelting we have examined a series of nucleoproteins depleted of different protein frac...

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Bibliographic Details
Published in:Nucleic acids research 1974-08, Vol.1 (8), p.1043-1058
Main Authors: Wilhelm, F. Xavier, Murcia, Gilbert M.de, Daune, Michel P.
Format: Article
Language:English
Subjects:
Animals
Biochemistry, Molecular Biology
Cattle
Chromatin
Chromatin - chemistry
Chromatin - isolation & purification
Chromosomal Proteins, Non-Histone
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - isolation & purification
Circular Dichroism
Histones
Histones - isolation & purification
In Vitro Techniques
Life Sciences
Lysine
Lysine - analysis
Nucleoproteins
Nucleoproteins - chemistry
Nucleoproteins - isolation & purification
Protein Conformation
Protein Denaturation
Spectrophotometry, Ultraviolet
Structural Biology
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Summary:In native nucleoprotein, the premelting structural changes of DNA are not observed by circular dichroism measurements. In order to determine which protein fraction of chromatin is responsible for the absence of premelting we have examined a series of nucleoproteins depleted of different protein fractions by treatment with sodium chloride or sodium deoxycholate. The premelting reappears as soon as non-histone proteins are removed or in residual complexes from which the two slightly lysine-rich histone fractions (F2a2+F2b) have been removed. On the other hand, it is shown that histone Fl alone is not able to suppress the premelting phenomenon. It is thus concluded that the absence of premelting is a property of native nucleoprotein where interactions between the different proteins complexed with DNA can occur and especially between the non-histone proteins and the two slightly lysine-rich histone fractions.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/1.8.1043