Open AccessHistone H5 promotes the association of condensed chromatin fragments to give pseudo‐higher‐order structures
Author(s) -
THOMAS Jean O.,
REES Christine,
PEARSON Edwin C.
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb08730.x
Subject(s) - chromatin , nucleosome , ionic strength , histone , chemistry , biophysics , histone h1 , dna , lysine , nuclease , divalent , crystallography , biochemistry , biology , aqueous solution , amino acid , organic chemistry
We describe two distinct situations in which chicken erythrocyte chromatin fragments associate in solution. The erythrocyte‐specific histone H5 is implicated since chromatins that do not contain H 5 do not show this behaviour.1 Well‐defined oligomers of between ∼ 6 and ∼ 18 nucleosomes prepared at low ionic strength condense and associate when the ionic strength is raised to 75 mM, forming pseudo‐higher‐order structures. The associated forms, probably predominantly dimers, are stabilized by migration of about 10% of the H 5, and of the minor lysine‐rich histone H 1, from the non‐associated forms, probably reflecting the preference of H 5 for higher‐order structures observed previously [Thomas, J. O. and Rees, C. (1983) Eur. J. Biochem. 134 , 109–115]. Since the final (H 1 + H 5) content of the aggregate at 75 mM is never higher than that of the fragment prepared at low ionic strength, migration is probably to a small proportion of sites that have inevitably become vacant due to handling losses at the higher (but not at low) ionic strength. H 5 thus maximizes its interactions in the condensed state of chromatin and even maintains the association of two or more fragments without continuity of the DNA. Aggregates of oligomers larger than about 18 nucleosomes may be too long to withstand hydrodynamic shear forces in the absence of such continuity. 2 During nuclease digestion of nuclear chromatin, H 5 and, to a lesser extent, H 1, are released from the ends of very short fragments and bind to larger oligomers of various sizes leading to heterogeneous aggregates that survive exposure to low ionic strength. These aggregates, in contrast to those described above, have up to 60% more H 5 and 20% more H 1 than chromatin prepared at low ionic strength. Whether the excess H 5 and H 1 bind non‐specifically or to a second low‐affinity binding site on each nucleosome is not known.The associated forms described above (1) are well defined and potentially useful for structural studies, whereas the other aggregates (2) seem less likely to be directly relevant to the native structure of chromatin.