Proteolytic Digestion Studies of Chromatin Core‐Histone Structure
Open Access
- 1 September 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 119 (1), 67-74
- https://doi.org/10.1111/j.1432-1033.1981.tb05577.x
Abstract
Trypsin digestion of chromatin results in a well‐defined set of limit peptides (P1‐P5) derived from the four core histones. Those from histones H3 and H4 have been identified. P1 is H3 residues 27‐129; P4 is H4 residues 18‐102 and P5 is H4 residues 20‐102. The N‐terminal sequences removed correlate well with the regions that undergo post‐synthetic acetylation and which show the greatest degree of sequence conservation. Autolytic digestion of chromatin releases a peptide (P1′) from H3 representing residues 21‐135. The implications of protease digestion of the higher order structure of chromatin are discussed.This publication has 34 references indexed in Scilit:
- The Histones of YeastEuropean Journal of Biochemistry, 1980
- Proteolytic Digestion Studies of Chromatin Core‐Histone StructureEuropean Journal of Biochemistry, 1980
- Primary organization of nucleosomes containing all five histories and DNA 175 and 165 base-pairs longJournal of Molecular Biology, 1980
- Amino acid sequence of two cyanogen bromide fragments of glycogen phosphorylaseBiochemistry, 1978
- Chromatin structure as probed by nucleases and proteases: Evidence for the central role of hitones H3 and H4Cell, 1976
- Preparation of Native Chromatin and Damage Caused by ShearingScience, 1975
- Proteolytic degradation of histones and site of cleavage in histone F2a1 and F3FEBS Letters, 1975
- Histone cross-complexing patternBiochemistry, 1974
- Purification of the five main calf thymus histone fractions by gel exclusion chromatographyFEBS Letters, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970