DNA topology in a chromatin model system
Copyright policy )DNA topology in a chromatin model system
The synthetic copolypeptide (Lys33, Leu67)100-Orn20, modeled on some general features of the histone sequences, has been found to supercoil the DNA double helix, wrapping it into a micelle, as a result of cohesive interactions between the polypeptide hydrophobic moieties. X-ray low-angle diffraction of complexes between the polypeptide and DNA is characterized by maxima at 50, 32, and 23 A, reminiscent of the chromatin pattern. The existence of a nucleosome-like structure along the DNA is suggested by gel electrophoresis analysis of DNA fragments after micrococcal nuclease digestion, showing the presence of a fragment of about 100 basepairs (bp) long. Topological experiments on the complexes with supercoiled as well as relaxed circular DNA by two-dimensional gel electrophoresis show the presence of left-handed superhelical turns. The results are in agreement with an intrinsic propensity of B-DNA to writhe into left-handed supercoils.
- Sapienza University of Rome Italy
- National Research Council Italy
Models, Genetic, DNA, Superhelical, Protein Conformation, DNA, Thymus Gland, Chromatin, copolypeptide modeled on histones; supercoiled DNA; X-ray low-angle diffraction; nucleosome structure; gel electrophoresis, X-Ray Diffraction, Escherichia coli, Animals, Nucleic Acid Conformation, Cattle, Peptides, Plasmids
Models, Genetic, DNA, Superhelical, Protein Conformation, DNA, Thymus Gland, Chromatin, copolypeptide modeled on histones; supercoiled DNA; X-ray low-angle diffraction; nucleosome structure; gel electrophoresis, X-Ray Diffraction, Escherichia coli, Animals, Nucleic Acid Conformation, Cattle, Peptides, Plasmids
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