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 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 F1 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.
Wilhelm
F X
FX
de Murcia
G M
GM
Daune
M P
MP
D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000737:chemistry / Q000302:isolation & purification; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry / Q000302:isolation & purification; D002942:Circular Dichroism; D006657:Histones / Q000302:isolation & purification; D066298:In Vitro Techniques; D008239:Lysine / Q000032:analysis; D009698:Nucleoproteins / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D011489:Protein Denaturation; D013056:Spectrophotometry, Ultraviolet
D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D009698:Nucleoproteins; D008239:Lysine