Sure, the new Apple products announced this week represented new breakthroughs and yes, you’ll be able to personalize these devices with countless modifications like cases, color and screens. The real action though, was unfolding (pun intended) in the world of chromatin analysis as a new method surfaced for introducing tags or native modifications into histones (or any other protein).
This accomplishment is now possible thanks to recent work published by Tom Muir and colleagues in Nature Chemistry.
Muir’s lab took a synthetic biology approach to introduce short tags and modifications into histone H2B using ultrafast split inteins – “naturally fractured proteins [from Cyanobacteria] that tightly associate and then rapidly catalyze protein trans-splicing (PTS)”. The approach is beautiful in that it is efficient and traceless, leaving only the desired tag or native modification in place. Muir and colleagues used H2B as a model protein to test the wonders of PTS both in vivo and in vitro. They find that:
- They could introduce tags and fluorescent probes into H2B both in vitro and in live cells
- Addition of tag/modification could be used to assess chromatin state (euchromatin vs. heterochromatin)
- H2BK120 ubiquitylation (a modification that cannot be mimicked with a simple mutation) can be introduced on native chromatin
- PTS-mediated H2BK120 ubiquitylation was functional and promoted H3K79me3
Overall, this new method is complementary to current approaches to study histones and their modifications in a native context while being limited to N- or C- termini. The authors say that in principle, any modification that can be introduced into a synthetic peptide can be introduced into a histone via PTS.
So what are you waiting for? Plug in to Nature Chemistry, May 2015 and get all the details.