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J. Biol. Chem., Vol. 265, Issue 26, 15572-15576, 09, 1990

Carboxyl methylation and COOH-terminal processing of the brain G- protein gamma-subunit

PS Backlund Jr, WF Simonds and AM Spiegel
Laboratory of General and Comparative Biochemistry, National Institute of Mental Health, National Institutes of Health, Bethesda, Maryland 20892.

The enzymatic methylation of the guanine nucleotide-binding proteins (G- proteins) gamma-subunit was investigated in brain membranes. Brain membranes were methylated in vitro using [3H-methyl]S- adenosylmethionine, and the G-protein beta gamma-complex was purified using an anti-beta antibody to assay for the protein during purification. The isolated G-protein beta gamma-complex was found to be carboxyl methylated on the gamma-subunit. The methyl group was localized by tryptic digestion to the carboxyl-terminal of the protein. The methylated tryptic peptides contained a modified cysteine and were very hydrophobic, suggesting additional modification by lipidation. The evidence suggests that the COOH-terminal of G-gamma is modified in a manner similar to the processing that occurs with the ras proteins.
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