Ribonuclease Z
| TRNase Z | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.26.11 | ||||||||
| CAS number | 98148-84-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
TRNase Z (EC 3.1.26.11, 3 tRNase, tRNA 3 endonuclease, RNase Z, 3' tRNase) is an enzyme.[1][2][3][4][5][6][7] Among other things, it catalyses the reactions involved in the maturation of tRNAs. Here, it endonucleolyticly cleaves the RNA and removes extra 3' nucleotides from the tRNA precursor, generating the 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule. Similarly, it processes tRNA-like molecules such as mascRNA.[8] The enzyme does not use a cofactor.
References
- ↑ Schiffer, S.; Rösch, S.; Marchfelder, A. (2002). "Assigning a function to a conserved group of proteins: the tRNA 3′-processing enzymes". EMBO J. 21 (11): 2769–2777. doi:10.1093/emboj/21.11.2769. PMC 126033
. PMID 12032089. - ↑ Mayer, M.; Schiffer, S.; Marchfelder, A. (2000). "tRNA 3′ processing in plants: nuclear and mitochondrial activities differ". Biochemistry. 39 (8): 2096–2105. doi:10.1021/bi992253e. PMID 10684660.
- ↑ Schiffer, S.; Helm, M.; Theobald-Dietrich, A.; Giege, R.; Marchfelder, A. (2001). "The plant tRNA 3′ processing enzyme has a broad substrate spectrum". Biochemistry. 40 (28): 8264–8272. doi:10.1021/bi0101953. PMID 11444972.
- ↑ Kunzmann, A.; Brennicke, A.; Marchfelder, A. (1998). "5′ end maturation and RNA editing have to precede tRNA 3′ processing in plant mitochondria". Proc. Natl. Acad. Sci. USA. 95 (1): 108–113. doi:10.1073/pnas.95.1.108. PMC 18142. PMID 9419337.
- ↑ Mörl, M.; Marchfelder, A. (2001). "The final cut. The importance of tRNA 3′-processing". EMBO Rep. 2 (1): 17–20. doi:10.1093/embo-reports/kve006. PMC 1083803. PMID 11252717.
- ↑ Minagawa, A.; Takaku, H.; Takagi, M.; Nashimoto, M. (2004). "A novel endonucleolytic mechanism to generate the CCA 3′ termini of tRNA molecules in Thermotoga maritima". J. Biol. Chem. 279 (15): 15688–15697. doi:10.1074/jbc.M313951200. PMID 14749326.
- ↑ Takaku, H.; Minagawa, A.; Takagi, M.; Nashimoto, M. (2003). "A candidate prostate cancer susceptibility gene encodes tRNA 3′ processing endoribonuclease". Nucleic Acids Res. 31 (9): 2272–2278. doi:10.1093/nar/gkg337. PMC 154223. PMID 12711671.
- ↑ Wilusz, JE.; Freier, SM.; Spector, DL (2008). "3′ end processing of a long nuclear-retained noncoding RNA yields a tRNA-like cytoplasmic RNA.". Cell. 135 (5): 919–932. doi:10.1016/j.cell.2008.10.012. PMC 2722846. PMID 19041754.
External links
- TRNase Z at the US National Library of Medicine Medical Subject Headings (MeSH)
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