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The binding of H1 (and H5) to nucleosome core particles was demonstrated by separating mononucleosomes according to their DNA size on acrylamide gels containing high molarity urea. The presence of urea causes a redistribution of H1 so that it associates with some particles of all linker lengths, including no linker. When the urea is removed the H1 remains associated with particles of all DNA sizes if the different size classes are not mixed with each other. Therefore, urea can effect the transfer of H1 from particles with linker to particles with no linker. When nucleosomes of uniform DNA fragment length, some containing and some lacking H1, are re-electrophoresed under native conditions, they migrate as two widely separated bands. The mobilities of these variants do not depend on linker length and are identical to the mobilities of native H1-containing and H1-lacking particles. When the same collection of particles is electrophoresed in the presence of high molarity urea they migrate with a uniform mobility. These results suggest that H1-containing nucleosomes are conformationally different from H1-lacking particles, but that this difference is eliminated when histone-histone interactions are disrupted by urea.
S A Newman, and
P Noon
June 2007,
DNA and cell biology,
S A Newman, and
P Noon
December 2021,
Current opinion in structural biology,
S A Newman, and
P Noon
April 2005,
The Journal of biological chemistry,
S A Newman, and
P Noon
May 2009,
Nucleic acids research,
S A Newman, and
P Noon
December 1998,
Biochimie,
S A Newman, and
P Noon
January 2013,
PLoS genetics,
S A Newman, and
P Noon
February 2012,
Nucleic acids research,
S A Newman, and
P Noon
February 2005,
DNA repair,
S A Newman, and
P Noon
June 2011,
Biomicrofluidics,
S A Newman, and
P Noon
January 1997,
Methods (San Diego, Calif.),
