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- W4283080265 endingPage "977" @default.
- W4283080265 startingPage "965" @default.
- W4283080265 abstract "Ribonuclease P (RNase P) enzymes are responsible for the 5' processing of tRNA precursors. In addition to the well-characterised ribozyme-based RNase P enzymes, an evolutionarily distinct group of protein-only RNase Ps exists. These proteinaceous RNase Ps (PRORPs) can be found in all three domains of life and can be divided into two structurally different types: eukaryotic and prokaryotic. Recent structural studies on members of both families reveal a surprising diversity of molecular architectures, but also highlight conceptual and mechanistic similarities. Here, we provide a comparison between the different types of PRORP enzymes and review how the combination of structural, biochemical, and biophysical studies has led to a molecular picture of protein-mediated tRNA processing." @default.
- W4283080265 created "2022-06-19" @default.
- W4283080265 creator A5019133588 @default.
- W4283080265 creator A5068015940 @default.
- W4283080265 date "2022-11-01" @default.
- W4283080265 modified "2023-10-14" @default.
- W4283080265 title "Structural and mechanistic basis of RNA processing by protein-only ribonuclease P enzymes" @default.
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- W4283080265 doi "https://doi.org/10.1016/j.tibs.2022.05.006" @default.
- W4283080265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35725940" @default.
- W4283080265 hasPublicationYear "2022" @default.
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