One key enzyme responsible for cutting the extra segment at the 5’ end of the tRNA is RNase P. Found in almost all life forms, this enzyme exists in two broad forms: one that is mostly made of ...

Thus, RNase likely unmasked the binding sites for the antibodies when removing RNA from antigens. As a result, more immune complexes formed and stimulated autoimmunity.

Figure 4. Non-canonical 3’ end processing of MALAT1 The MEN β long nuclear-retained noncoding RNA, also known as NEAT1_2, is similarly processed at its 3’ end by RNase P. Surprisingly, although ...

One such mechanism, termed RNase-based self-incompatibility, employs ribonucleases as the pistil component. Although it is widespread, it has only been characterised in a handful of distantly related ...

The p.E265* variant of RNASEL was produced as a truncated protein and displayed LOF, while the p.I264V variant exhibited neutral expression and function. P1's OAS1 variant showed LOF, while P2, P3 ...

More information: Takamasa Teramoto et al, Structural basis of transfer RNA processing by bacterial minimal RNase P, Nature Communications (2025). DOI: 10.1038/s41467-025-60002-1 ...