Studies on the Role and Mode of Operation of the Very‐Lysine‐Rich Histones in Eukaryote Chromatin
- 1 December 1977
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 81 (3), 499-505
- https://doi.org/10.1111/j.1432-1033.1977.tb11975.x
Abstract
270 MHz PMR was used to study the effect of phosphorylation of histone H1 [calf thymus] in vitro on the structure of isolated H1 molecules and on the interaction of H1 with DNA. Phosphorylation at serine-105, which is located in the globular region of H1, reduced the enthalpy of structure formation from 24 .+-. 2 kcal mol-1 (100 .+-. 8 kJ mol-1) to 13 .+-. 2 kcal mol-1 (55 .+-. 8 kJ mol-1). Phosphorylation at either or both serine-37 and serine-105 reduced the binding strength of the histone to DNA considerably at some ionic strengths.This publication has 18 references indexed in Scilit:
- A comparison of the structure of chicken erythrocytef and chicken liver chromatinCell, 1976
- The subunit structure of chromatin from Physarum polycephalumNucleic Acids Research, 1976
- The DNA repeat lengths in chromatins from sea urchin sperm and gastrula cells are markedly differentFEBS Letters, 1976
- Organisation of subunits in chromatinNucleic Acids Research, 1976
- Nucleosome structure in Aspergillus nidulansCell, 1976
- Differences and similarities in chromatin structure of neurospora crassa and higher eucaryotesCell, 1976
- Solenoidal model for superstructure in chromatin.Proceedings of the National Academy of Sciences, 1976
- Selective synthesis and modification of nuclear proteins during maturation of avian erythroid cellsArchives of Biochemistry and Biophysics, 1976
- Control of Cell Division by Very Lysine Rich Histone (F1) PhosphorylationNature, 1974
- Magnetic Resonance Studies of DeoxyribonucleoproteinNature, 1973