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• W2052912295 abstract "Protein arginylation and arginine methylation are two posttranslational modifications of emerging importance that involve Arg residues and their modifications. To test a hypothesis that posttranslationally added arginines can be methylated, we used high-precision mass spectrometry and metabolic labeling to find whether posttranslationally added arginines can serve as methylation sites. We identified a number of proteins in vivo, on which posttranslationally added Arg have undergone mono- and dimethylation. This double modification predominantly affects the chromatin-containing nuclear fraction and likely plays an important regulatory role in chromatin-associated proteins. Moreover, inhibition of arginylation and Arg methylation results in a significant reduction of the nucleus size in cultured cells, suggesting changes in chromatin compaction and nuclear architecture. Our findings suggest a functional link between protein regulation by arginylation and methylation that affects nuclear structure in vivo." @default.
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• W2052912295 date "2011-11-01" @default.
• W2052912295 modified "2023-09-30" @default.
• W2052912295 title "Arginylation and Methylation Double Up to Regulate Nuclear Proteins and Nuclear Architecture In Vivo" @default.
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• W2052912295 doi "https://doi.org/10.1016/j.chembiol.2011.08.019" @default.
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