Abstract
Lysine methylation is an important post-translational modification that affects protein function; for example, the transcriptional activity of the p53 tumor suppressor protein. To facilitate structural characterization of complexes involving proteins and methylated targets by nuclear magnetic resonance spectroscopy, we devised a simple method for preparing recombinant 15N/13C-enriched peptides with a 13C-methyl- labeled methylated lysine analogue. The method, which relies on the synthesis of 13C-enriched alkylating agents, was applied to the production of 15-residue p53 peptides variously methylated at lysine analogue 370. The peptides were used to probe the methylation state-dependent interactions of mono, di, and trimethylated p53 with three different proteins.
Original language | English (US) |
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Pages (from-to) | 3798-3800 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 48 |
Issue number | 18 |
DOIs | |
State | Published - May 12 2009 |
ASJC Scopus subject areas
- Biochemistry