Histone H1 and chromatin higher order structure. Does histone H1 exhibit specific self-association?
1. Histones H1 and H5 in chromatin and in free solution can be cross-linked to higher multimers. Is this due to a specific protein/protein interaction? If so, this interaction might be the structural basis of the condensation of the chromosomal nucleofilament, known to be mediated by histones H1 and H5. 2. Since only the central domain of H1 and H5 exhibits tertiary folding and globular structure, this is the most likely site of specific interaction. 3. Formaldehyde has been used to test whether the central domains of histone H1 from calf thymus or from sea urchin sperm or histone H5 from chicken erythrocytes self-interact. 4. The cross-linking shown by each globular peptide was compared with that of its parent histone. 5. In all three cases the peptide cross-linked to a much lower extent than its intact parent histone and the observed cross-linked rates were roughly in proportion to the relative number of lysine residues parent histone and peptide. 6. It is concluded that there is no specific self-interaction between the globular domains of either H1 or H5 molecules in free solution. 7. This result suggests that specific H1/H1 protein/protein interactions are not the basic cause of chromatin condensation.
D000818:Animals; D002417:Cattle; D002645:Chickens; D002843:Chromatin / Q000378:metabolism* / Q000648:ultrastructure; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism*; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D011487:Protein Conformation; D012617:Sea Urchins; D013045:Species Specificity; D013094:Spermatozoa / Q000378:metabolism
D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances