Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide

Article Abstract:

The histone acetyltransferase (HAT) domain of Tetrahymena GCN5 may contain protein surfaces that are contacted by protein cofactors to modulate its acetylation activity. Some residues conserved within the GCN5/PCAF subfamily of HAT proteins are accessible for protein cofactor interaction in the ternary tGCN5/CoA/histone H3 complex. These residues cluster directly above and flanking the histone H3 binding site, as well as being more widely distributed over the bottom/C-terminal surface of the protein. It is suggested that GNAT proteins use their structurally divergent N- and C-terminal segments for CoA-dependent substrate-specific binding.

Protein binding

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Steroid receptor coactivator-1 is a histone acetyltransferase

Article Abstract:

Genetic research shows that the steroid-receptor coactivator SRC-1 exhibits histone acetyltransferase (HAT) activity which binds with the histone acetyltransferase p300/CBP-associated factor (PCAF). PCAF and SRC-1 cause acetylation in histones. Genetic mapping techniques indicate that the HAT domain is found between residues 1,107 and 1,216. Experimental techniques are described including human SRC-1 monoclonal antibody and western blot analysis.

Genetic aspects, Steroid hormones, Steroid receptors

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Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A

Article Abstract:

The solution structure of tGCN5 catalytic domain in complex with coenzyme A has been determined. The structure consists of the amino-terminal domain similar to those of other GCN5-related N-acetyltransferases, and the carboxy-terminal domain. Coenzyme A binds between the two domains, and chemical shift changes on titration with histone H3 peptides suggest a binding site at the domain boundary opposite coenzyme A.

Coenzymes

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