RSC unravels the nucleosome.
RSC and SWI/SNF chromatin-remodeling complexes were previously reported to generate a stably altered nucleosome. We now describe the formation of hybrids between nucleosomes of different sizes, showing that the stably altered structure is a noncovalent dimer. A basis for dimer formation is suggested by an effect of RSC on the supercoiling of closed, circular arrays of nucleosomes. The effect may be explained by the interaction of RSC with DNA at the ends of the nucleosome, which could lead to the release 60--80 bp or more from the ends. DNA released in this way may be trapped in the stable dimer or lead to alternative fates such as histone octamer transfer to another DNA or sliding along the same DNA molecule.
Lorch
Y
Y
Department of Structural Biology, Stanford School of Medicine, Stanford, CA 94305, USA.
Zhang
M
M
Kornberg
R D
RD
D000818:Animals; D002843:Chromatin / Q000235:genetics / Q000378:metabolism; D004278:DNA, Superhelical / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D019281:Dimerization; D029721:Drosophila Proteins; D006657:Histones / Q000235:genetics / Q000378:metabolism; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D016601:RNA-Binding Proteins; D051381:Rats; D017412:Ribonucleoprotein, U1 Small Nuclear / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism*; D014982:Xenopus laevis
D002843:Chromatin; D004278:DNA, Superhelical; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D006657:Histones; D009707:Nucleosomes; D016601:RNA-Binding Proteins; C103337:RSC complex, S cerevisiae; D017412:Ribonucleoprotein, U1 Small Nuclear; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; C089969:snf protein, Drosophila