Abstract
Catalytic complexes of nuclear ribonuclease P (RNase P) ribonucleoproteins are composed of several protein subunits that appear to have specific roles in enzyme function in tRNA processing. This review describes recent progress made in the characterization of human RNase P, its relationship with the ribosomal RNA processing ribonucleoprotein RNase MRP, and the unexpected evolutionary conservation of its subunits. A new model for the biosynthesis of human RNase P is presented, in which this process is dynamic, transcription-dependent, and implicates functionally distinct nuclear compartments in tRNA biogenesis.
| Original language | English |
|---|---|
| Pages (from-to) | 1-7 |
| Number of pages | 7 |
| Journal | RNA |
| Volume | 8 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2002 |
Keywords
- Cajal bodies
- Catalytic ribonucleoprotein
- Nucleolus
- RNase MRP
- RNase P
- tRNA
Fingerprint
Dive into the research topics of 'Human ribonuclease P: Subunits, function, and intranuclear localization'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver