Dynamics of unfolded nucleosomal fiber.
The "rigidity" of chromatin fiber solenoidal structure in different states of condensation was evaluated with the help of gel-electrophoresis. A new property of the unfolded nucleosomal fiber-the capacity to condense with temperature-was demonstrated. These results together with our previously obtained data (W.A. Krajewski et al., Mol. Gen. Genet. 230, pp. 442-448, 1991; W.A. Krajewski et al., Ibid. 231, pp. 17-22, 1991) testify that changes in DNA linking number of transcriptionally active minichromosomes arise in vivo from alteration of nucleosomal solenoid parameters (i.e. from supernucleosomal level of chromatin organization), rather than from core histone modifications only or from increased flexibility of DNA within nucleosomes.
Krajewski
W A
WA
Laboratory of Biochemistry, Russian Academy of Sciences, Moscow.
Panin
V M
VM
Razin
S V
SV
D000818:Animals; D002458:Cell Fractionation; D002843:Chromatin / Q000648:ultrastructure*; D004247:DNA / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000302:isolation & purification; D008099:Liver / Q000378:metabolism; D008961:Models, Structural; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000648:ultrastructure*; D051381:Rats; D014158:Transcription, Genetic
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D004247:DNA