Ribonuclease T
Not to be confused with ribonuclease T1 or ribonuclease T2.
| Ribonuclease T | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 A ribonuclease T dimer in complex with DNA (orange), from PDB ID 3NH1.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | rnt | ||||||||
| Pfam | PF00929 | ||||||||
| InterPro | IPR013520 | ||||||||
| SMART | SM00479 | ||||||||
| |||||||||
Ribonuclease T (RNase T, exonuclease T, exo T) is a ribonuclease enzyme involved in the maturation of transfer RNA and ribosomal RNA in bacteria,[2] as well as in DNA repair pathways.[3] It is a member of the DnaQ family of exonucleases and non-processively acts on the 3' end of single-stranded nucleic acids. RNase T is capable of cleaving both DNA and RNA, with extreme sequence specificity discriminating against cytosine at the 3' end of the substrate.[1][2]
References
- 1 2 Hsiao, Y.-Y.; Duh, Y.; Chen, Y.-P.; Wang, Y.-T.; Yuan, H. S. (2012). "How an exonuclease decides where to stop in trimming of nucleic acids: Crystal structures of RNase T-product complexes". Nucleic Acids Research. 40 (16): 8144–54. doi:10.1093/nar/gks548. PMID 22718982.
- 1 2 Zuo, Y.; Deutscher, M. P. (2002). "The Physiological Role of RNase T Can Be Explained by Its Unusual Substrate Specificity". Journal of Biological Chemistry. 277 (33): 29654–61. doi:10.1074/jbc.M204252200. PMID 12050169.
- ↑ Hsiao, Yu-Yuan; Fang, Woei-Horng; Lee, Chia-Chia; Chen, Yi-Ping; Yuan, Hanna S. (2014). "Structural Insights into DNA Repair by RNase T—An Exonuclease Processing 3′ End of Structured DNA in Repair Pathways". PLoS Biology. 12 (3): e1001803. doi:10.1371/journal.pbio.1001803. PMC 3942315
. PMID 24594808.
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