DNA-protein complexes of the nuclear matrix: visualization and partial characterization of the protein component.
Complexes composed of DNA attached to the nuclear matrix and of proteins most tightly bound to DNA are visualized as globular particles 25-35 nm in diameter. Their morphology depends greatly on the isolation conditions: a Cs salts/urea combination permits the isolation while CsCl/sarcosyl destroys the particles. The preparation is shown to have the same protein content regardless of the treatment employed. The proteins of the complex are resistant to SDS and pronase treatment and to phenol/chloroform extraction while being associated with DNA.
Chernokhvostov
V V
VV
Engelhardt Institute of Molecular Biology, Moscow, USSR.
Stel'mashchuk VYa
Razin
S V
SV
Georgiev
G P
GP
D000818:Animals; D002458:Cell Fractionation / Q000379:methods; D002460:Cell Line; D002467:Cell Nucleus / Q000648:ultrastructure*; D004247:DNA / Q000378:metabolism* / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000302:isolation & purification / Q000648:ultrastructure; D051379:Mice; D009687:Nuclear Proteins / Q000302:isolation & purification* / Q000648:ultrastructure; D009690:Nucleic Acid Conformation; D010316:Particle Size; D010954:Plasmacytoma
D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D004247:DNA