The DOI matches its Crossref record; 111 of the 111 references it cites were found in a registry or an index.
RIBONUCLEASE P: Unity and Diversity in a tRNA Processing Ribozyme
Abstract
Ribonuclease P (RNase P) is the endoribonuclease that generates the mature 5′-ends of tRNA by removal of the 5′-leader elements of precursor-tRNAs. This enzyme has been characterized from representatives of all three domains of life (Archaea, Bacteria, and Eucarya) ( 1 ) as well as from mitochondria and chloroplasts. The cellular and mitochondrial RNase Ps are ribonucleoproteins, whereas the most extensively studied chloroplast RNase P (from spinach) is composed solely of protein. Remarkably, the RNA subunit of bacterial RNase P is catalytically active in vitro in the absence of the protein subunit ( 2 ). Although RNA-only activity has not been demonstrated for the archaeal, eucaryal, or mitochondrial RNAs, comparative sequence analysis has established that these RNAs are homologous (of common ancestry) to bacterial RNA. RNase P holoenzymes vary greatly in organizational complexity across the phylogenetic domains, primarily because of differences in the RNase P protein subunits: Mitochondrial, archaeal, and eucaryal holoenzymes contain larger, and perhaps more numerous, protein subunits than do the bacterial holoenzymes. However, that the nonbacterial RNase P RNAs retain significant structural similarity to their catalytically active bacterial counterparts indicates that the RNA remains the catalytic center of the enzyme.
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Cited by
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Metadata
- Authors
- Frank, D. N., & Pace, N. R.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1998-06
- Volume
- 67
- Issue
- 1
- Pages
- 153-180
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2111332566
- Cited by
- 465
- References
- 111
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Open access
- closed
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- Frank, D. N., & Pace, N. R. (1998). RIBONUCLEASE P: Unity and Diversity in a tRNA Processing Ribozyme. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.67.1.153
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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