title: Higher-order structure of Saccharomyces cerevisiae chromatin.
abstract: We have developed a method for partially purifying chromatin from Saccharomyces cerevisiae (baker's yeast) to a level suitable for studies of its higher-order folding. This has required the use of yeast strains that are free of the ubiquitous yeast "killer" virus. Results from dynamic light scattering, electron microscopy, and x-ray diffraction show that the yeast chromatin undergoes a cation-dependent folding into 30-nm filaments that resemble those characteristic of higher-cell chromatin; moreover, the packing of nucleosomes within the yeast 30-nm filaments is similar to that of higher cells. These results imply that yeast has a protein or protein domain that serves the role of the histone H 1 found in higher cells; physical and genetic studies of the yeast activity could help elucidate the structure and function of H 1. Images of the yeast 30-nm filaments can be used to test crossed-linker models for 30-nm filament structure.
authors.affiliation: Department of Chemistry, University of Illinois, Urbana 61801.
authors.forename: P T
authors.initials: PT
authors.lastname: Lowary
authors.forename: J
authors.initials: J
authors.lastname: Widom
mesh_terms: D000818:Animals; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D002645:Chickens; D002843:Chromatin / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure*; D004912:Erythrocytes / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D008027:Light; D008854:Microscopy, Electron; D012441:Saccharomyces cerevisiae / Q000378:metabolism / Q000648:ultrastructure*; D012542:Scattering, Radiation; D012964:Sodium / Q000494:pharmacology; D013104:Spheroplasts / Q000648:ultrastructure; D014961:X-Ray Diffraction
chemical_list: D002843:Chromatin; D006657:Histones; D012964:Sodium