Ribonuclease T1 (RNase T1)

Ribonuclease T1 (RNase T1) is a small, 104-amino acid fungal endonuclease originally isolated from the mold Aspergillus oryzae [2, 20]. It is characterized by its high specificity for cleaving single-stranded RNA at the 3'-phosphodiester bond of guanine residues, a property that has made it an indispensable tool in molecular biology for RNA sequencing, fingerprinting, and structural studies [4, 11]. The enzyme's catalytic mechanism involves a two-step process: a transphosphorylation reaction forming a 2',3'-cyclic phosphate intermediate, followed by hydrolysis to a 3'-phosphate [1, 3, 20]. Due to its potent ribonucleolytic activity, RNase T1 and its derivatives have been explored as potential 'ribotoxins' for cancer therapy, where they can induce apoptosis by degrading cellular RNA and halting protein synthesis [3, 15, 18]. Despite this therapeutic potential, challenges such as immunogenicity and the requirement for targeted delivery to avoid non-specific toxicity remain significant hurdles [3, 15]. Additionally, RNase T1 serves as a prominent model system in biochemistry for studying protein folding, stability, and enzyme-substrate interactions [2, 20].

Other names

Guanyl-specific ribonuclease T1GuanyloribonucleaseAspergillus oryzae ribonucleaserntARNase T1

Cleavage of 3',5'-phosphodiester bonds of RNA specifically at guanine residues via a 2',3'-cyclic phosphate intermediate.