An Asymmetric Model for the Nucleosome: A Binding Site for Linker Histones Inside the DNA Gyres

• Published in: Science (American Association for the Advancement of Science) Vol. 274; no. 5287; pp. 614 - 617
• Main Authors: Pruss, Dmitry, Bartholomew, Blaine, Persinger, Jim, Hayes, Jeffrey, Arents, Gina, Moudrianakis, Evangelos N., Wolffe, Alan P.
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 25.10.1996; American Association for the Advancement of Science; The American Association for the Advancement of Science
• Subjects: Animals; Base Sequence; Binding Sites; Biological and medical sciences; Chromatin; Chromatin. Chromosome; Cross-Linking Reagents; Deoxyribonucleic acid; DNA; DNA - chemistry; DNA - metabolism; DNA probes; Dyadic relations; Electrophoresis; Fundamental and applied biological sciences. Psychology; Gels; Histones; Histones - chemistry; Histones - metabolism; Models, Molecular; Molecular and cellular biology; Molecular biology; Molecular genetics; Molecular Sequence Data; Molecules; Nucleic Acid Conformation; Nucleosomes; Nucleosomes - chemistry; Nucleotides; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins - chemistry; RNA, Ribosomal - genetics; Xenopus; Molecular arrangement; Molecular structure; Nucleosome; Xenopus laevis; Amphibia; Molecular interaction; Crosslinking; Salientia; Binding site; Core particle; Vertebrata; Superhelical structure; DNA; Histone; Nuclear protein
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.274.5287.614

Histone-DNA contacts within a nucleosome influence the function of trans-acting factors and the molecular machines required to activate the transcription process. The internal architecture of a positioned nucleosome has now been probed with the use of photo-activatable cross-linking reagents to determine the placement of histones along the DNA molecule. A model for the nucleosome is proposed in which the winged-helix domain of the linker histone is asymmetrically located inside the gyres of DNA that also wrap around the core histones. This domain extends the path of the protein superhelix to one side of the core particle.