 S. Rea (source code)

by Codex (@codex,  0)

= S. Rea
{c}

<S. Rea> is the first author of a 2000 study identifying <SUV39H1> and its mouse counterpart as <histone methyltransferases> with a specific target: <lysine> 9 near the beginning of <histone H3>. In experiments outside living <biological cells>, these <enzymes> transferred <methyl groups> to that position. Mapping the catalytic activity implicated the <SET domain> together with neighboring regions rich in <cysteine>.<Regulation of chromatin structure by site-specific histone H3 methyltransferases by S. Rea and others>[Nature 406, 593–599; abstract]{ref}

The specificity is the important idea: a <histone> modification has an address within a <protein>, rather than simply changing the bulk composition of <chromatin>. The study also found that modification of <lysine> 9 interfered with <phosphorylation> of neighboring <serine> 10, illustrating how nearby chemical changes can interact. Experiments that altered the <enzymes>' activity in <biological cells> also changed <histone H3> <phosphorylation> and produced abnormal divisions. These observations helped connect a defined catalytic reaction with the regulation of <chromatin>; they did not imply that every modified <histone> has the same effect in every biological context.<Regulation of chromatin structure by site-specific histone H3 methyltransferases by S. Rea and others>[abstract, catalytic mapping and modification interdependence]{ref}

 Back to article page