Preparation of recombinant peptides with site- and degree-specific lysine13C-methylation

Gaofeng Cui, Maria Victoria Botuyan, Georges Mer

Research output: Contribution to journalArticle

10 Scopus citations

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 languageEnglish (US)
Pages (from-to)3798-3800
Number of pages3
JournalBiochemistry
Volume48
Issue number18
DOIs
StatePublished - May 12 2009

ASJC Scopus subject areas

  • Biochemistry

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