Abstract
We have previously reported that the catalytic RNA subunit of ribonuclease P (RNase P) of Escherichia coli (M1 RNA) cleaves Drosophila initiator methionine tRNA (tRNA(i)Met), alanine tRNA (tRNA(Ala)) and histidine tRNA (tRNA(His)) within the mature tRNA sequences to produce specific fragments. We call this further cleavage hyperprocessing. These cleavages were dependent on the occurrence of altered conformations of the tRNAs. Here, we found that the RNase P RNA of Bacillus subtilis can hyperprocess these three tRNAs at the same sites as does M1 RNA. The hyperprocessing activity may probably be common feature for Bacterial RNase P RNAs.
| Original language | English |
|---|---|
| Title of host publication | Nucleic acids research. Supplement (2001) |
| Pages | 209-210 |
| Number of pages | 2 |
| Edition | 1 |
| Publication status | Published - 2001 |
| Externally published | Yes |