In class we talked about using unnatural amino acid mutagenesis to site-specifically modify histones. This review article talks about that method as well as several others. Solid-phase peptide synthesis can be used to create relatively short pieces of histones with the proper modifications. This technique is great for high-throughput screening with proteins thought to bind histones. The problem is that some of the interactions may be context-specific. Native chemical ligation (NCL) can be used to join peptides together, but length is still a factor. Expressed protein ligation (EPL) is a similar technique in which recombinant proteins can be cleaved and joined to synthetic peptides. The next step is to study the effects of multiple different modifications on the same nucleosome, as well as the effects of asymmetric modification of neighboring nucleosomes.
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