Philadelphia -- For the first time, scientists working in The Wistar Institute laboratory of Ronen Marmorstein, PhD, in collaboration with Shelley Berger, PhD, have determined the three-dimensional structure of a key enzyme involved in gene activation. In nature, this enzyme, which is called GCN5, functions to attach acetyl groups to histone proteins that are bound to DNA to facilitate gene activation. The Marmorstein group has obtained a structure of the histone acetyltransferase (HAT) domain of GCN5 bound to both its histone target and to its coenzyme-A cofactor. Details of this structure appear in the paper, "Crystal structure of Tetrahymena GCN5 with bound coenzyme-A and histone H3 peptide," in the September 2, 1999 issue of Nature.
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