Resistance of chromatin superstructure to tryptic digestion modulated by conjugated polyacrylamide
- 27 June 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 157 (1) , 111-114
- https://doi.org/10.1016/0014-5793(83)81126-0
Abstract
Soluble polyacrylamide conjugates have been used to modulate tryptic digestion of chromatin. Digestion of histones H1/H5 and H3 are mutually dependent and relatively independent of that of the core histones which are not significantly digested until 50–60% of H3 is degraded. H1/H5 and H3 are most exposed, H3 behaves as a ‘non‐core’ histone, its destruction appears to be the critical factor in the collapse of the chromatin superstructure during tryptic digestions. The digestion kinetics are explained by proposing that the initial sites of attack are in cavities much larger than the diameter of trypsin (4–5 nm). Procedures for the preparation of soluble polyacrylamide and its conjugation to trypsin are described.Keywords
This publication has 16 references indexed in Scilit:
- ChromatinAnnual Review of Biochemistry, 1982
- Chromatin superstructure: The next level of structure above the nucleosome has an alternating character. A two-nucleosome based series is generated by probes armed with DNAase-I acting on isolated nucleiBiochemical and Biophysical Research Communications, 1981
- The structure of histone H1 and its location in chromatinNature, 1980
- Nucleosome StructureAnnual Review of Biochemistry, 1980
- Chromatin core particle unfolding induced by tryptic cleavage of histonesNucleic Acids Research, 1977
- Chromatin structure as probed by nucleases and proteases: Evidence for the central role of hitones H3 and H4Cell, 1976
- The use of proteolytic enzymes to determine the location of histones in chromosomal substructuresArchives of Biochemistry and Biophysics, 1976
- Histones H2a, H2b, H3, and H4 form a tetrameric complex in solutions of high saltCell, 1975
- The Modification of Deoxyribonucleohistone by Trypsin and ChymotrypsinEuropean Journal of Biochemistry, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970