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Acetyltransferases are enzymes that transfer acetyl (CH3C=O) groups to proteins, generally on lysine residues. This post-translational modification has regulatory roles, notably in chromatin structure and function.
N-terminal acetylation is a common eukaryotic protein modification that is primarily catalysed by the N-acetyl transferase complex A (NatA). Here, the authors present the crystal structure of NatA bound to Huntingtin yeast two-hybrid protein K (HypK) and show that HypK is a negative regulator of NatA.
N-terminal acetylation is a common protein modification in eukaryotes. Here the authors show that in Arabidopsis, N-terminal acetylation is decreased by drought stress, that abundance of an N-terminal acetyltransferase is reduced by abscisic acid and that constitutive downregulation can confer drought resistance.