Abstract
We report here the structure of the putative chromo domain from MOF, a member of the MYST family of histone acetyltransferases that acetylates histone H4 at Lys-16 and is part of the dosage compensation complex in Drosophila. We found that the structure of this domain is a beta-barrel that is distinct from the alpha + beta fold of the canonical chromo domain. Despite the differences, there are similarities that support an evolutionary relationship between the two domains, and we propose the name "chromo barrel." The chromo barrel domains may be divided into two groups, MSL3-like and MOF-like, on the basis of whether a group of conserved aromatic residues is present or not. The structure suggests that, although the MOF-like domains may have a role in RNA binding, the MSL3-like domains could instead bind methylated residues. The MOF chromo barrel shares a common fold with other chromatin-associated modules, including the MBT-like repeat, Tudor, and PWWP domains. This structural similarity suggests a probable evolutionary pathway from these other modules to the canonical chromo domains (or vice versa) with the chromo barrel domain representing an intermediate structure.
Highlights
We report here the structure of the putative chromo domain from MOF, a member of the MYST family of histone acetyltransferases that acetylates histone H4 at Lys-16 and is part of the dosage compensation complex in Drosophila
We found that the structure of this domain is a -barrel that is distinct from the ␣ ؉  fold of the canonical chromo domain
The chromo domain was originally defined as a region of homology between heterochromatin protein 1 (HP1)3 and Polycomb (Pc) [1] and is found in many other chromatin-associated proteins [2, 3]
Summary
Expression and Purification of the MOF Chromo Barrel Domain— The DNA sequence corresponding to amino acids 367– 454 of Drosophila MOF was inserted into the NdeI and BamHI sites of the pET15b vector (Novagen). The vector was transformed into the expression strain Escherichia coli TUNER (DE3) pLacI (Novagen) and the protein purified using standard methods (see supplemental information)
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