دورية أكاديمية
The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions
العنوان: | The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions |
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المؤلفون: | Bradley P. Klemm, Nancy Wu, Yu Chen, Xin Liu, Kipchumba J. Kaitany, Michael J. Howard, Carol A. Fierke |
المصدر: | Biomolecules, Vol 6, Iss 2, p 27 (2016) |
بيانات النشر: | MDPI AG, 2016. |
سنة النشر: | 2016 |
المجموعة: | LCC:Microbiology |
مصطلحات موضوعية: | RNase P, ribozyme, PRORP, endonuclease, tRNA maturation, tRNA recognition, Microbiology, QR1-502 |
الوصف: | Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5’ end maturation in precursor transfer RNAs. Since its discovery in the 1970s, RNase P enzymes have been identified and studied throughout the three domains of life. Interestingly, RNase P is either RNA-based, with a catalytic RNA subunit, or a protein-only (PRORP) enzyme with differential evolutionary distribution. The available structural data, including the active site data, provides insight into catalysis and substrate recognition. The hydrolytic and kinetic mechanisms of the two forms of RNase P enzymes are similar, yet features unique to the RNA-based and PRORP enzymes are consistent with different evolutionary origins. The various RNase P enzymes, in addition to their primary role in tRNA 5’ maturation, catalyze cleavage of a variety of alternative substrates, indicating a diversification of RNase P function in vivo. The review concludes with a discussion of recent advances and interesting research directions in the field. |
نوع الوثيقة: | article |
وصف الملف: | electronic resource |
اللغة: | English |
تدمد: | 2218-273X 84558814 |
Relation: | http://www.mdpi.com/2218-273X/6/2/27; https://doaj.org/toc/2218-273X |
DOI: | 10.3390/biom6020027 |
URL الوصول: | https://doaj.org/article/e2ae747c1db8455881486b85482053b5 |
رقم الأكسشن: | edsdoj.2ae747c1db8455881486b85482053b5 |
قاعدة البيانات: | Directory of Open Access Journals |
تدمد: | 2218273X 84558814 |
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DOI: | 10.3390/biom6020027 |