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The Glutamine Residue of the Conserved GGQ Motif inSaccharomyces cerevisiaeRelease Factor eRF1 Is Methylated by the Product of theYDR140wGene
2004
Journal of Biological Chemistry
Polypeptide release factors from eubacteria and eukaryotes, although similar in function, belong to different protein families. They share one sequence motif, a GGQ tripeptide that is vital to release factor (RF) activity in both kingdoms. In bacteria, the Gln residue of the motif in RF1 and RF2 is modified to N 5 -methyl-Gln by the S-adenosyl L-methionine-dependent methyltransferase PrmC and the absence of Gln methylation decreases the release activity of Escherichia coli RF2 in vitro
doi:10.1074/jbc.m407252200
pmid:15509572
fatcat:gnww7jgomnfhvawpllvonz2sja