دورية أكاديمية

The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions

التفاصيل البيبلوغرافية
العنوان: The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions
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
الوصف
تدمد:2218273X
84558814
DOI:10.3390/biom6020027