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J Am Chem Soc. 2013 Feb 27;135(8):2879-82. doi: 10.1021/ja3108214. Epub 2013 Feb 19.

Site-specific and regiospecific installation of methylarginine analogues into recombinant histones and insights into effector protein binding.

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Chemistry and Chemical Biology Graduate Program, University of California, San Francisco, 600 16th Street, MC2280, San Francisco, California 94158, USA.


Arginine methylation has emerged as a widespread post-translational modification with influence over myriad cellular processes. However, the molecular mechanisms underlying such methylarginine-dependent phenomena remain unclear. To aid in this research, a facile method was developed to install methylarginine analogues on recombinant protein for use in biochemical, biophysical, and structural studies. Through chemical conjugation of novel α,β-unsaturated amidine precursors with proteins, methylarginine mimics can be displayed with control of methylation site, extent, and regiospecificity. Analogue installation into histones using this strategy produced modified proteins that were recognized by antibodies specific to endogenous methylarginine, and these histones retained the capacity to form mononucleosomes. Moreover, a native methylarginine-specific binding domain was shown to interact with methylarginine analogue-modified substrates. This chemical conjugation method for installing methylarginine analogues provides an efficient route to produce homogeneous modified proteins for subsequent investigations of methylarginine-dependent processes.

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