Lysine pyrrolation is a naturally-occurring covalent modification involved in the production of DNA mimic proteins.

ABSTRACT: Covalent modification of proteins exerts significant effects on their chemical properties and has important functional and regulatory consequences. We now report the identification and verification of an electrically-active form of modified proteins recognized by a group of small molecules commonly used to interact with DNA. This previously unreported property of proteins was initially discovered when the γ-ketoaldehydes were identified as a source of the proteins stained by the DNA intercalators. Using 1,4-butanedial, the simplest γ-ketoaldehyde, we characterized the structural and chemical criteria governing the recognition of the modified proteins by the DNA intercalators and identified N(ε)-pyrrolelysine as a key adduct. Unexpectedly, the pyrrolation conferred an electronegativity and

SUBMITTER: Miyashita H 

PROVIDER: S-EPMC4061549 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature