The role that lysine methylation of ribosomal and ribosomal-associated proteins plays in regulating the process of translation is poorly understood compared to its role in regulating other processes such as transcription. The purpose of this proposal is to identify novel protein lysine methyltransferases in Saccharomyces cerevisiae that may be involved in regulating translation. This will be accomplished by analyzing knockout strains in which putative SET domain-containing genes have been deleted. SET domain-containing methyltransferases are lysine methyltransferases that have been shown to post-translationally modify proteins such as cytochrome c, Rubisco, and histones. During a search of the Protein Family Database, seven genes encoding putative lysine methyltransferases were found, one of which I have already determined to encode a ribosomal protein lysine methyltransferase, which I now refer to as RKM1.
One aim of this proposal will be to determine whether the remaining genes that have the closest homology to RKM1 also encode ribosomal protein lysine methyltransferases. Once the substrates are identified I plan to determine the role the methyltransferase plays in the regulation of its substrate and subsequently translation.
| Porras-Yakushi, Tanya R; Whitelegge, Julian P; Clarke, Steven (2007) Yeast ribosomal/cytochrome c SET domain methyltransferase subfamily: identification of Rpl23ab methylation sites and recognition motifs. J Biol Chem 282:12368-76 |
| Porras-Yakushi, Tanya R; Whitelegge, Julian P; Clarke, Steven (2006) A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10. J Biol Chem 281:35835-45 |
