| SYNTHESIS |
Making histones bearing acetyl, methyl groups A new method to synthesize histone proteins with acetyl and methyl groups attached to specific amino-acid side chains will help biochemists figure out the function of these modifications in vivo. To pack their genome into a small space, cells wrap their DNA around beads made of four different histone proteins. These "beads on a string" further condense to form a higher order structure called chromatin. The timing and pattern of posttranslational modifications--including methylation, acetylation, and phosphorylation--made to the exposed tails of histone proteins control protein recruitment and DNA accessibility for transcription. A team led by assistant professor Dewey G. McCafferty of the University of Pennsylvania Medical School now reports a method to make fully functional synthetic histones containing site-specific modifications [Proc. Natl. Acad. Sci. USA, 100, 12033 (2003)]. Unlike previous attempts to make modified histones, "our method allows us to prepare any histone with any modification pattern," McCafferty tells C&EN. He hopes to use the synthetic histones to probe the specificity and mechanisms of histone modification enzymes |
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