Yeast inner histones and the evolutionary conservation of histone-histone interactions.
The inner histones of the yeast, Saccharomyces cerevisiae, have been isolated and identified by their amino acid compositions. H4 appears to be close to its calf and pea counterparts. H2a, H2b, and H3 have diverged. The isolation of the histones was accomplished by consecutive slab-gel fractionation, and a number of novel features of the method are described. These appear to be generally useful for preparing many types of protein. The binding pattern of the yeast inner histones is identical to the binding pattern for calf and for pea histones. Data on interspecies complexing indicate that the surfaces across which the histones interact are very highly conserved.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005075:Biological Evolution; D002417:Cattle; D002942:Circular Dichroism; D006657:Histones / Q000302:isolation & purification; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D013045:Species Specificity
D000596:Amino Acids; D006657:Histones; D046911:Macromolecular Substances