tRNase Z
- PMID:17305600
- DOI: 10.2174/092986607779816050
tRNase Z
Abstract
Endonuclease tRNase Z catalyzes the generation of the mature 3' end of tRNA precursors through specific endonucleolytic cleavage. The enzyme has been characterized from organisms representative of all domains of life as well as from organelles, and the crystal structure of three bacterial enzymes has been determined. This review presents an overview of its properties and what is known about its structure, substrate recognition, cleavage site definition, and potential practical applications.
Similar articles
- Crystal structure of the tRNA 3' processing endoribonuclease tRNase Z from Thermotoga maritima.Ishii R, Minagawa A, Takaku H, Takagi M, Nashimoto M, Yokoyama S.Ishii R, et al.J Biol Chem. 2005 Apr 8;280(14):14138-44. doi: 10.1074/jbc.M500355200. Epub 2005 Jan 27.J Biol Chem. 2005.PMID:15701599
- The flexible arm of tRNase Z is not essential for pre-tRNA binding but affects cleavage site selection.Minagawa A, Ishii R, Takaku H, Yokoyama S, Nashimoto M.Minagawa A, et al.J Mol Biol. 2008 Aug 29;381(2):289-99. doi: 10.1016/j.jmb.2008.05.016. Epub 2008 May 15.J Mol Biol. 2008.PMID:18602113
- The N-terminal half-domain of the long form of tRNase Z is required for the RNase 65 activity.Takaku H, Minagawa A, Takagi M, Nashimoto M.Takaku H, et al.Nucleic Acids Res. 2004 Aug 18;32(15):4429-38. doi: 10.1093/nar/gkh774. Print 2004.Nucleic Acids Res. 2004.PMID:15317868Free PMC article.
- tRNase Z: the end is not in sight.Späth B, Canino G, Marchfelder A.Späth B, et al.Cell Mol Life Sci. 2007 Sep;64(18):2404-12. doi: 10.1007/s00018-007-7160-5.Cell Mol Life Sci. 2007.PMID:17599240Free PMC article.Review.
- The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties.Vogel A, Schilling O, Späth B, Marchfelder A.Vogel A, et al.Biol Chem. 2005 Dec;386(12):1253-64. doi: 10.1515/BC.2005.142.Biol Chem. 2005.PMID:16336119Review.
Cited by
- Biogenesis, Functions, Interactions, and Resources of Non-Coding RNAs in Plants.Chao H, Hu Y, Zhao L, Xin S, Ni Q, Zhang P, Chen M.Chao H, et al.Int J Mol Sci. 2022 Mar 28;23(7):3695. doi: 10.3390/ijms23073695.Int J Mol Sci. 2022.PMID:35409060Free PMC article.Review.
- Extracellular vesicles-associated tRNA-derived fragments (tRFs): biogenesis, biological functions, and their role as potential biomarkers in human diseases.Weng Q, Wang Y, Xie Y, Yu X, Zhang S, Ge J, Li Z, Ye G, Guo J.Weng Q, et al.J Mol Med (Berl). 2022 May;100(5):679-695. doi: 10.1007/s00109-022-02189-0. Epub 2022 Mar 24.J Mol Med (Berl). 2022.PMID:35322869Free PMC article.Review.
- Identification and analysis of candidate fungal tRNA 3'-end processing endonucleases tRNase Zs, homologs of the putative prostate cancer susceptibility protein ELAC2.Zhao W, Yu H, Li S, Huang Y.Zhao W, et al.BMC Evol Biol. 2010 Sep 6;10:272. doi: 10.1186/1471-2148-10-272.BMC Evol Biol. 2010.PMID:20819227Free PMC article.
- Biological function and clinical application prospect of tsRNAs in digestive system biology and pathology.Du J, Huang T, Zheng Z, Fang S, Deng H, Liu K.Du J, et al.Cell Commun Signal. 2023 Oct 30;21(1):302. doi: 10.1186/s12964-023-01341-8.Cell Commun Signal. 2023.PMID:37904174Free PMC article.Review.
- A survey of green plant tRNA 3'-end processing enzyme tRNase Zs, homologs of the candidate prostate cancer susceptibility protein ELAC2.Fan L, Wang Z, Liu J, Guo W, Yan J, Huang Y.Fan L, et al.BMC Evol Biol. 2011 Jul 23;11:219. doi: 10.1186/1471-2148-11-219.BMC Evol Biol. 2011.PMID:21781332Free PMC article.
Publication types
MeSH terms
Substances
Related information
LinkOut - more resources
Full Text Sources