High impact information on RPL30

• The RPL32 substrate, bound to L32, forms a complex with U1 snRNP, the first step in spliceosome assembly [1].
• A temperature-sensitive exo84 mutation caused increased ratios of pre-mRNA to mRNA for the Rpl30 and actin transcripts in cells incubated at the non-permissive temperature [2].
• Eventually, the unspliced RPL30 transcripts escape the grasp of L30, associate with ribosomes, and fall prey to nonsense mediated decay [3].
• Two in vitro selection experiments were conducted to determine the RNA sequence requirements for binding ribosomal protein L32 (RPL32) from Saccharomyces cerevisiae [4].
• Yeast ribosomal protein L32, RPL32, specifically represses splicing by binding to a purine-rich asymmetric loop adjacent to the 5' splice site of its own transcript [5].

Biological context of RPL30

• Like other protein-lysine N-methyltransferases, the methylase of YL32 exhibits a high substrate specificity [6].

Associations of RPL30 with chemical compounds

• Methyl groups could be transferred in vitro to proteins YL23 and YL32 in extracts from cultures of an S-adenosyl methionine auxotroph deprived of the methyl-group donor [7].
• In the most heavily methylated proteins the methylated amino acids formed in vitro were the same as those found in vivo (monomethyllysine and dimethyllysine in YL32; dimethyl and trimethyllsine in YL23) [7].

References