Cancer Institute A national cancer institute
designated cancer center

Peter Sarnow

Publication Details

  • A histone H4-specific methyltransferase. Properties, specificity and effects on nucleosomal histones.

    Sarnow P, Rasched I, Knippers R. Biochim Biophys Acta. 1981; 655 (3): 349-58

    A histone H4-specific methyltransferase was purified 80-100-fold from nuclei of calf lymphocytes and from calf thymus. Some biochemical properties of the enzyme are described. The enzyme transfers in vitro methyl groups from S-adenosylmethionine preferentially to the lysine residue 20 of histone H4. This is the major in vivo methylation site of H4. DNA-bound or nucleosomal H4 is not methylated in vitro. We have used methylated and unmodified H4 (in the presence of sufficient quantities of the other core histones) for nucleosome reconstitution in vitro and have not found significant differences in the efficiencies of assembly.

    PubMedID: 7284392

Stanford Medicine Resources:

Footer Links: