In vivo studies on yeast cytochrome c methylation in relation to protein synthesis.

Methylation of cytochrome c was studied in vivo using double label with L-[methyl-3H]methionine and DL-[2-14C]methionine. In pulse-chase experiments the cytochrome c associated with the mitochondrial fraction possessed a higher ratio of 3H/14C label, suggesting the presence of methylated cytochrome c. The appearance of methylated cytochrome c in mitochondria showed no lag phase. The inhibition of cytochrome c methylation in presence of cycloheximide indicated that both the methylation and protein synthesis were tightly coupled and cycloheximide selectively inhibited cytochrome c methylation. There was also an indication of selective turnover of incorporation methyl groups in preformed cytochrome c.