By CIBA Foundation Staff
Chapter 1 Foreword: Histone Nomenclature (pages 1–6): E. M. Bradbury
Chapter 2 advent (pages 5–6): E. L. Smith
Chapter three Chromosornal constitution as obvious by means of Electron Microscopy (pages 7–28): Hans Ris
Chapter four the explicit Template job of Chromatin (pages 29–57): G. Felsenfeld, R. Axel, H. Cedar and B. Sollner?Webb
Chapter five Histone functionality and Evolution as considered by way of series reviews (pages 59–76): Robert J. Delange and Emil L. Smith
Chapter 6 constitution of Histone H2A (Histone ALK, IIbl or F2a2) (pages 77–93): P. Sautiere, D. Wouters?Tyrou, B. Laine and G. Biserte
Chapter 7 Chromosomal Proteins on the topic of Histones (pages 95–112): E. W. Johns, G. H. Goodwin, J. M. Walker and C. Sanders
Chapter eight Chemistry of the Non?Histone Chromosomal Proteins (pages 113–130): Sarah C. R. Elgin and William E. Stumph
Chapter nine Histones in Chromosomal constitution and keep an eye on of cellphone department (pages 131–155): E. M. Bradbury
Chapter 10 X?Ray Diffraction of Nucleohistones from Spermatozoa (pages 157–174): Juan A. Subirana, Luis C. Puigjaner, Josep Roca, Remedios Llopis And and Pedro Suau
Chapter eleven The Regulatory function of Non?Histone Proteins in RNA Synthesis (pages 181–198): J. Paul and R. S. Gilmour
Chapter 12 Sequence?Specific Binding of DNA through Non?Histone Proteins and Their Migration from Cytoplasm to Nucleus in the course of Gene Activation (pages 199–228): Vincent G. Allfrey, Akira Inoue, Jonathan Karn, Edward M. Johnson, Robert A. solid and John W. Hadden
Chapter thirteen The organic Roles of Post?Synthetic differences of easy Nuclear Proteins (pages 229–258): G. H. Dixon, E. P. M. Candido, B. M. Honda, A. J. Louie, A. R. Macleod and M. T. Sung
Chapter 14 Micromodification of Histone in the course of the mobilephone Cycle (pages 259–267): Margery G. Ord and Lloyd A. Stocken
Chapter 15 alterations in Chromatin constitution and serve as in W138 Cells encouraged to Proliferate (pages 269–289): Renato Baserga, Bernd Bombik and Claudio Nicolini
Chapter sixteen The association of Histone Complexes alongside the Chromosomal Fibre (pages 291–313): Harold Weintraub, Frederick Van Lente and Richard Blumenthal
Chapter 17 legislation of Gene Expression in better Organisms: the way it All Works (pages 315–351): James Bonner
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Additional info for Ciba Foundation Symposium 28 - The Structure and Function of Chromatin
11-21, Elsevier, Amsterdam RIS,H. (1968) Effect of fixation on the dimension of nucleohistone fibres. J. Cell Biol. 39, 158a-159b RIS, H. ), pp. 221-249, North-Holland, Amsterdam RIS, H. F. (1970) Chromosome structure. Annu. Rev. Genet. 4,263-294 SIMPSON, R. T. (1971) Modification of chromatin with acetic anhydride. J. (1971) Experimental changes in the width of chromatin fibres from chicken erythrocytes. Exp. Cell Res. 67, 161-170 SORSA, M. & SORSA, V. (1967) Electron microscopic observations on interband fibrils in Drosophila salivary chromosomes.
Weintraub: After treating chromatin with increasing concentrations of formaldehyde and monitoring the cross-linked products on sodium dodecyl sulphate gels, J. Jackson in my laboratory finds that specific oligomers can be formed, but only by about 10% of the total histone. Although all histone is cross-linked into high molecular weight material, treatment with deoxyribonuclease regenerates most of the histones, thereby indicating that most formaldehyde cross-linking is probably between DNA and protein.
I shall finally comment on the model of Clark & Felsenfeld (1971), since it conflicts with mine. Their model involves lengths of about 200 base-pairs of SPECIFIC TEMPLATE ACTIVITY 47 histone-covered DNA alternating with comparable lengths of completely free DNA. The basis for the model is the observation that about half the DNA in chromatin is degraded by staphylococcal nuclease to acid-soluble form, while the remaining half is protected from nuclease action. Briefly, I attribute this observation to cleavage by the nuclease in regions of histone-associated DNA, leading to release of the histone, degradation of the DNA to acid-soluble form, and rebinding of the histone to intact regions which are, as a consequence, fully protected from nuclease action.