RNase P: increased versatility through protein complexity?
| Autor: | David R. Engelke, Michael C. Marvin |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
RNA
Untranslated Exosome complex RNase P RNase PH Ribonuclease P Article RNA Transfer Animals Humans RNA Small Nucleolar RNA Catalytic Signal recognition particle RNA RNA Messenger RNase H Molecular Biology Conserved Sequence Binding Sites biology Ribozyme Cell Biology Non-coding RNA Molecular biology Introns RNA Bacterial RNase MRP Biochemistry biology.protein Nucleic Acid Conformation RNA |
| Zdroj: | RNA Biology. 6:40-42 |
| ISSN: | 1555-8584 1547-6286 |
| DOI: | 10.4161/rna.6.1.7566 |
| Popis: | Ribonuclease P (RNase P) is an essential enzyme that catalyzes the 5' endonucleolytic cleavage of precursor transfer RNAs (pre-tRNAs). It is found in all phylogenetic domains: bacteria, archaea and eukaryotes. The bacterial enzyme consists of a single, catalytic RNA subunit and one small protein, while the archaeal and eukaryotic enzymes have 4–10 proteins in addition to a similar RNA subunit. The bacterial RNA acts as a ribozyme at high salt in vitro; however the added protein optimizes kinetics and makes specific contacts with the pre-tRNA substrate. The bacterial protein subunit also appears to be required for the processing of non-tRNA substrates by broadening recognition tolerance. In addition, the immense increase in protein content in the eukaryotic enzymes suggests substantially enlarged capacity for recognition of additional substrates. Recently intron-encoded box C/D snoRNAs were shown to be likely substrates for RNase P, with several lines of evidence suggesting that the nuclear holoenzyme binds tightly to, and can cleave single-stranded RNA in a sequence dependent fashion. The possible involvement of RNase P in additional RNA processing or turnover pathways would be consistent with previous findings that RNase MRP, a variant of RNase P that has evolved to participate in ribosomal RNA processing, is also involved in turnover of specific messenger RNAs. Here, involvement of RNase P in multiple RNA processing pathways is discussed. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|