Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P
Ribonuclease P efficiently processes all tRNA precursors despite sequence variation at the site of cleavage. Here, authors use high-throughput enzymology and cryoEM to reveal conformational changes that drive recognition by bacterial RNase P.
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-32843-7 |
| _version_ | 1828345692368666624 |
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| author | Jiaqiang Zhu Wei Huang Jing Zhao Loc Huynh Derek J. Taylor Michael E. Harris |
| author_facet | Jiaqiang Zhu Wei Huang Jing Zhao Loc Huynh Derek J. Taylor Michael E. Harris |
| author_sort | Jiaqiang Zhu |
| collection | DOAJ |
| description | Ribonuclease P efficiently processes all tRNA precursors despite sequence variation at the site of cleavage. Here, authors use high-throughput enzymology and cryoEM to reveal conformational changes that drive recognition by bacterial RNase P. |
| first_indexed | 2024-04-14T00:15:30Z |
| format | Article |
| id | doaj.art-cec6aa07037546878427f7c421ca776b |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-14T00:15:30Z |
| publishDate | 2022-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-cec6aa07037546878427f7c421ca776b2022-12-22T02:23:09ZengNature PortfolioNature Communications2041-17232022-08-0113111310.1038/s41467-022-32843-7Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease PJiaqiang Zhu0Wei Huang1Jing Zhao2Loc Huynh3Derek J. Taylor4Michael E. Harris5Department of Chemistry, University of FloridaDepartment of Pharmacology, Case Western Reserve University School of MedicineDepartment of Chemistry, University of FloridaDepartment of Chemistry, University of FloridaDepartment of Pharmacology, Case Western Reserve University School of MedicineDepartment of Chemistry, University of FloridaRibonuclease P efficiently processes all tRNA precursors despite sequence variation at the site of cleavage. Here, authors use high-throughput enzymology and cryoEM to reveal conformational changes that drive recognition by bacterial RNase P.https://doi.org/10.1038/s41467-022-32843-7 |
| spellingShingle | Jiaqiang Zhu Wei Huang Jing Zhao Loc Huynh Derek J. Taylor Michael E. Harris Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P Nature Communications |
| title | Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P |
| title_full | Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P |
| title_fullStr | Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P |
| title_full_unstemmed | Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P |
| title_short | Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P |
| title_sort | structural and mechanistic basis for recognition of alternative trna precursor substrates by bacterial ribonuclease p |
| url | https://doi.org/10.1038/s41467-022-32843-7 |
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