Abstract
The physical and functional links between transcription and processing machines of tRNA in the cell remain essentially unknown. We show here that whole HeLa extracts depleted of ribonuclease P (RNase P), a tRNA-processing ribonucleoprotein, exhibit a severe deficiency in RNA polymerase (Pol) III transcription of tRNA and other small, noncoding RNA genes. However, transcription can be restored by the addition of a purified holoenzyme. Targeted cleavage of the H1 RNA moiety of RNase P alters enzyme specificity and diminishes Pol III transcription. Moreover, inactivation of RNase P by targeting its protein subunits for destruction using small interfering RNAs inhibits Pol III function and Pol III-directed promoter activity in the cell. RNase P exerts its role in transcription through association with Pol III and chromatin of active tRNA and 5S rRNA genes. The results demonstrate a role for RNase P in Pol III transcription and suggest that transcription and early processing of tRNA may be coordinated.
Original language | English |
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Pages (from-to) | 1621-1635 |
Number of pages | 15 |
Journal | Genes and Development |
Volume | 20 |
Issue number | 12 |
DOIs | |
State | Published - 15 Jun 2006 |
Keywords
- Catalytic ribonucleoprotein
- RNA polymerase III
- RNase P
- Small, noncoding RNA gene
- tRNA processing