Open AccessThe reconstitution of a hybrid histone octamer containing avian 110 Cys‐des‐thio‐histone H3 and sea‐urchin 73 Cys‐histone H4
Author(s) -
GREYLING H. Johann,
SEWELL B. Trevor,
HOLT Claus
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb13845.x
Subject(s) - histone octamer , histone h2a , histone , histone h3 , histone methylation , histone code , chemistry , histone h1 , histone methyltransferase , chromatosome , biochemistry , nucleosome , biology , microbiology and biotechnology , dna , dna methylation , gene , gene expression
A hybrid histone octamer was reconstituted from eythrocyte H2A and H2B, avian [ 110 Cys ‐des‐thio]histone H3 and the sea‐urchin sperm [ 73 Cys]H4 variant. [ 110 Cys ‐Des‐thio]histone H3 was prepared by reaction of natural H3 with Raney nickel. The ability of the hybrid octamer to crystallise to the same form as the natural octamer demonstrated that the chemical modification of cysteine to alanine in H3 and the mutation from threonine to cysteine in sperm H4 do not alter histone‐histone interactions in the octamer. Since the sulfhydryl groups of both H4 molecules are fully accessible to 5,5′‐dithiobis(2‐nitrobenzoate) these residues provide suitable sites for the introduction of a single cysteine‐specific label per H4 molecule in the octamer.