Robust repression of tRNA gene transcription during stress requires protein arginine methylation
| Autor: | Christopher A. Jackson, Michael C. Yu, Richoo B. Davis, Tao Liu, Neah Likhite |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Protein-Arginine N-Methyltransferases
Saccharomyces cerevisiae Proteins Transcription Genetic Health Toxicology and Mutagenesis Protein subunit Repressor Saccharomyces cerevisiae Plant Science Arginine Methylation Biochemistry Genetics and Molecular Biology (miscellaneous) RNA polymerase III 03 medical and health sciences RNA Transfer Stress Physiological Transcription (biology) Gene Expression Regulation Fungal Amino Acid Sequence Research Articles 030304 developmental biology Regulation of gene expression 0303 health sciences Ecology Chemistry 030302 biochemistry & molecular biology RNA Polymerase III RNA Cell biology Repressor Proteins Protein Subunits Mutation Transfer RNA Research Article Protein Binding |
| Zdroj: | Life Science Alliance |
| ISSN: | 2575-1077 |
| Popis: | This work examines how protein arginine methylation of Rpc31, a subunit of RNA Pol III, promotes negative regulation of tRNA biogenesis in the context of cellular stress. Protein arginine methylation is an important means by which protein function can be regulated. In the budding yeast, this modification is catalyzed by the major protein arginine methyltransferase Hmt1. Here, we provide evidence that the Hmt1-mediated methylation of Rpc31, a subunit of RNA polymerase III, plays context-dependent roles in tRNA gene transcription: under conditions optimal for growth, it positively regulates tRNA gene transcription, and in the setting of stress, it promotes robust transcriptional repression. In the context of stress, methylation of Rpc31 allows for its optimal interaction with RNA polymerase III global repressor Maf1. Interestingly, mammalian Hmt1 homologue is able to methylate one of Rpc31’s human homologue, RPC32β, but not its paralogue, RPC32α. Our data led us to propose an efficient model whereby protein arginine methylation facilitates metabolic economy and coordinates protein-synthetic capacity. |
| Databáze: | OpenAIRE |
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