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- W2897089610 abstract "The RNA exosome is a conserved multi-subunit complex essential for processing and degradation of several types of RNAs. Although many of the functions of the RNA exosome are well established, whether the activity of this complex is regulated remains unclear. Here we performed a proteomic analysis of the RNA exosome complex purified from Schizosaccharomyces pombe and identified 39 post-translational modifications (PTMs), including phosphorylation, methylation, and acetylation sites. Interestingly, most of the modifications were identified in Dis3, a catalytic subunit of the RNA exosome, as well as in the exosome-associated RNA helicase, Mtr4. Functional analysis of selected PTM sites using modification-deficient and -mimetic versions of exosome subunits revealed substitutions that affected cell growth and exosome functions. Notably, our results suggest that site-specific phosphorylation in the catalytic center of Dis3 and in the helical bundle domain of Mtr4 control their activity. Our findings support a view in which post-translational modifications fine-tune exosome activity and add a layer of regulation to RNA degradation." @default.
- W2897089610 created "2018-10-26" @default.
- W2897089610 creator A5019011415 @default.
- W2897089610 creator A5041114334 @default.
- W2897089610 creator A5074584877 @default.
- W2897089610 date "2018-10-13" @default.
- W2897089610 modified "2023-10-18" @default.
- W2897089610 title "Proteomic profiling and functional characterization of post-translational modifications of the fission yeast RNA exosome" @default.
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- W2897089610 doi "https://doi.org/10.1093/nar/gky915" @default.
- W2897089610 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6265454" @default.
- W2897089610 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30321377" @default.
- W2897089610 hasPublicationYear "2018" @default.
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