Abstract
Chromatin plays an important role in the regulation of gene expression. Covalent modification of the tails of the histone proteins, which make up the nucleosome around which DNA is wrapped, can alter the response of a gene to the transcription machinery. For example, methylation of Lys 9 in the tail of histone H3 results in epigenetic repression of gene expression. The chromodomain-containing protein HP1 binds to methylated Lys 9 , but it has not been clear why only a subset of chromodomain-containing proteins interact with chromatin. Jacobs and Khorasanizadeh have determined the structure of the HP1 chromodomain bound to a methylated H3 tail. The methylammonium group is recognized by a hydrophobic cage in HP1, and the H3 tail completes the β-sandwich architecture of the chromodomain. S. A. Jacobs, S. Khorasanizadeh, Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295 , 2080-2083 (2002). [Abstract] [Full Text]
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
