Front cover of the journal "Nucleic Acids Research" Volume 42 Issue 2 2014
Research from the School of Pharmacy published in the journal Nucleic Acids Research has been selected as a Breakthrough Article by the editorial board (among the top 2% of publications annually). The research (a collaboration between the Gene Regulation and Structural Biology groups) describes four crystal structures of a chromatin recognition domain in complex with the N-terminal tail of histone H3. The study reveals for the first time that histone tails can adopt a ‘helix-hinge’ conformation when in complex with a chromatin regulatory protein, enabling the sampling of histone modifications such as lysine acetylation and methylation that affect gene expression (the histone code). The ‘reader’ protein, in this case, is the histone acetyltransferase MOZ that is implicated in leukaemia, thus the molecular structures will aid efforts to develop targeted therapeutics as anti- cancer agents.
The work was selected for the Cover Image of the January 2014 issue of NAR http://nar.oxfordjournals.org/content/42/2.cover-expansion
and is available as an Open Access publication.
Dreveney I, Deeves SD, Fulton J, Yue B, Messmer M, Bhattacharya A, Collins HM & Heery DM (2014). NAR Breakthrough Article : The DOUBLE PHD Finger Domain of MOZ/MYST3 induces a-helical fold of the histone H3 tail to facilitate acetylation and methylation sampling and modification
Nucleic Acids Research 42, (2) 822-835.
Posted on Thursday 6th February 2014