The surprise PR domain of FOG1
[ PDB file ] [ PubMed link ]
Many years ago, Gerd and I spotted a section of FOG1 outside the ZFs that looked like it might have been ordered. After only 12 years or so, Joel finally finished solving the structure of the domain (which is only ~110 residues, so who knows *why* it took him so long!). It turns out to be a PR domain - a fold that is essentially the same as the SET domains that act as methyltransferases - mostly adding methyl groups tolysines at the N-terminal tails of histones. This means that FOG1 is *potentially* an enzyme, although we were unable to demonstrate methyltransferase activity (via a collaboration with Masoud Vedadi in Toronto). It also makes FOG1 a member of a family of 16 other human proteins that contain this domain - some of which *have* been demonstrated to be enzymes. So, we shall see...