Three-dimensional structure of extended chromatin fibers as revealed by tapping-mode scanning force microscopy
| Autor: | Bruno Samorì, K. E. Van Holde, Jordanka Zlatanova, Guoliang Yang, Charles H. Robert, Sanford H. Leuba, Carlos Bustamante |
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| Přispěvatelé: | Department of Chemistry, University of Oregon, University of Oregon [Eugene], Department of Biochemistry and Biophysics, Oregon State University (OSU), Howard Hughes Medical Institute (HHMI) |
| Rok vydání: | 1994 |
| Předmět: |
Sodium Chloride
Microscopy Atomic Force Models Biological Scanning Force Microscope Histones Fixatives 03 medical and health sciences chemistry.chemical_compound Low salt Animals Nucleosome Scanning Force Microscopy [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences Multidisciplinary biology Chemistry Osmolar Concentration 030302 biochemistry & molecular biology Chromatin Low ionic strength Crystallography Histone Biophysics biology.protein Glutaraldehyde Chickens Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 1994, 91 (24), pp.11621-11625. ⟨10.1073/pnas.91.24.11621⟩ |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | Unfixed chicken erythrocyte chromatin fibers in very low salt have been imaged with a scanning force microscope operating in the tapping mode in air at ambient humidity. These images reveal a three-dimensional organization of the fibers. The planar "zig-zag" conformation is rare, and extended "beads-on-a-string" fibers are seen only in chromatin depleted of histones H1 and H5. Glutaraldehyde fixation reveals very similar structures. Fibers fixed in 10 mM salt appear somewhat more compacted. These results, when compared with modeling studies, suggest that chromatin fibers may exist as irregular three-dimensional arrays of nucleosomes even at low ionic strength. |
| Databáze: | OpenAIRE |
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