Abstract
The present studies establish the enzymatic methylation of lysine residues in certain proteins with S-adenosylmethionine as the methyl donor. Ribosomal proteins of the aquatic fungus Blastocladiella emersonii and basic proteins of chromatin from Ehrlich ascites carcinoma cell nuclei were shown to act as methyl acceptors. Crude protein preparations from Salmonella typhimurium were also able to accept methyl groups. In each case, only lysine residues in protein were methylated to yield e-N-methyllysine. The product of this reaction proved to be identical with authentic e-N-methyllysine by paper electrophoresis and column chromatography.
Highlights
MethodsSeveral changes of water at O”, and chromatographed on carboxymethyl cellulose according to the method of Waller [8] or Phillips and Johns [9]
The present studies establish the enzymatic methylation of lysine residues in certain proteins with S-adenosylmethionine as the methyl donor
The amino acid e-iV-methyllysine has been shown to be a major constituent of Salmonella typhimurium flagellar protein [1]
Summary
Several changes of water at O”, and chromatographed on carboxymethyl cellulose according to the method of Waller [8] or Phillips and Johns [9]. The latter procedure was modified in that all of the solutions contained 6 M urea. The amino acid composition of ribosomal protein from B. emersonii was determined on 20-hour hydrolysates (6 N HCl, 110”, Nz) with the Spinco amino acid analyzer (model 120) by the procedure of Moore, Spackman, and Stein [10]. The short column (15 cm) was used for the separation of e-N-methyllysine from the other basic amino acids. In certain cases the column effluent was collected directly in l.O-ml fractions so that radioactivity and ninhydrin determinations could be performed on each fraction
Sign-in/Register to view highlights & summary 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 callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
