The Methylation of Lysine Residues in Protein

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 a...

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Bibliographic Details
Published in:The Journal of biological chemistry 1966-04, Vol.241 (8), p.1857-1862
Main Authors: Comb, D G, Sarkar, N, Pinzino, C J
Format: Article
Language:English
Subjects:
Alkylation
Animals
Bacterial Proteins - metabolism
Carcinoma, Ehrlich Tumor - metabolism
Chromatography
Electrophoresis
Fungi - metabolism
In Vitro Techniques
Lysine - metabolism
Methionine
Neoplasm Proteins - metabolism
Proteins - metabolism
Ribosomes - metabolism
Salmonella typhimurium
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Summary: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 ε- N -methyllysine. The product of this reaction proved to be identical with authentic ε- N -methyllysine by paper electrophoresis and column chromatography.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(18)96714-1