| 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]
- ^ a b Hsiao YY, Duh Y, Chen YP, Wang YT, Yuan HS (September 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. PMC 3439924. PMID 22718982.
- ^ a b Zuo Y, Deutscher MP (August 2002). "The physiological role of RNase T can be explained by its unusual substrate specificity". The Journal of Biological Chemistry. 277 (33): 29654–61. doi:10.1074/jbc.M204252200. PMID 12050169.
- ^ Hsiao YY, Fang WH, Lee CC, Chen YP, Yuan HS (March 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.