Article ; Online: The specificity landscape of bacterial ribonuclease P.
The Journal of biological chemistry
2023 Volume 300, Issue 1, Page(s) 105498
Abstract: ... emerging for bacterial ribonucleoprotein RNase P a widespread and essential tRNA 5' processing endonuclease ... the well-established structure and kinetics of bacterial RNase P enabled the development of high throughput ... substrate as well as the RNA and protein subunits of bacterial RNase P during binding ...
| Abstract | Developing quantitative models of substrate specificity for RNA processing enzymes is a key step toward understanding their biology and guiding applications in biotechnology and biomedicine. Optimally, models to predict relative rate constants for alternative substrates should integrate an understanding of structures of the enzyme bound to "fast" and "slow" substrates, large datasets of rate constants for alternative substrates, and transcriptomic data identifying in vivo processing sites. Such data are either available or emerging for bacterial ribonucleoprotein RNase P a widespread and essential tRNA 5' processing endonuclease, thus making it a valuable model system for investigating principles of biological specificity. Indeed, the well-established structure and kinetics of bacterial RNase P enabled the development of high throughput measurements of rate constants for tRNA variants and provided the necessary framework for quantitative specificity modeling. Several studies document the importance of conformational changes in the precursor tRNA substrate as well as the RNA and protein subunits of bacterial RNase P during binding, although the functional roles and dynamics are still being resolved. Recently, results from cryo-EM studies of E. coli RNase P with alternative precursor tRNAs are revealing prospective mechanistic relationships between conformational changes and substrate specificity. Yet, extensive uncharted territory remains, including leveraging these advances for drug discovery, achieving a complete accounting of RNase P substrates, and understanding how the cellular context contributes to RNA processing specificity in vivo. |
|---|---|
| MeSH term(s) | Escherichia coli/enzymology ; Escherichia coli/genetics ; Nucleic Acid Conformation ; Ribonuclease P/chemistry ; Ribonuclease P/genetics ; Ribonuclease P/metabolism ; RNA Precursors/classification ; RNA Precursors/metabolism ; RNA, Bacterial/genetics ; RNA, Bacterial/metabolism ; RNA, Transfer/genetics ; RNA, Transfer/metabolism ; Substrate Specificity ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Protein Binding |
| Chemical Substances | Ribonuclease P (EC 3.1.26.5) ; RNA Precursors ; RNA, Bacterial ; RNA, Transfer (9014-25-9) ; Bacterial Proteins |
| Language | English |
| Publishing date | 2023-11-25 |
| Publishing country | United States |
| Document type | Journal Article ; Review |
| ZDB-ID | 2997-x |
| ISSN | 1083-351X ; 0021-9258 |
| ISSN (online) | 1083-351X |
| ISSN | 0021-9258 |
| DOI | 10.1016/j.jbc.2023.105498 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
More links
Kategorien
In stock of ZB MED Cologne/Königswinter
| Uc I Zs.108: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG) |
Order via subito
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.