Unknown

Dataset Information

0

Eukaryotic RNase P RNA mediates cleavage in the absence of protein.


ABSTRACT: The universally conserved ribonucleoprotein RNase P is involved in the processing of tRNA precursor transcripts. RNase P consists of one RNA and, depending on its origin, a variable number of protein subunits. Catalytic activity of the RNA moiety so far has been demonstrated only for bacterial and some archaeal RNase P RNAs but not for their eukaryotic counterparts. Here, we show that RNase P RNAs from humans and the lower eukaryote Giardia lamblia mediate cleavage of four tRNA precursors and a model RNA hairpin loop substrate in the absence of protein. Compared with bacterial RNase P RNA, the rate of cleavage (k(obs)) was five to six orders of magnitude lower, whereas the affinity for the substrate (appK(d)) was reduced approximately 20- to 50-fold. We conclude that the RNA-based catalytic activity of RNase P has been preserved during evolution. This finding opens previously undescribed ways to study the role of the different proteins subunits of eukaryotic RNase P.

SUBMITTER: Kikovska E 

PROVIDER: S-EPMC1892975 | BioStudies | 2007-01-01T00:00:00Z

REPOSITORIES: biostudies

Similar Datasets

2011-01-01 | S-EPMC3153969 | BioStudies
2008-01-01 | S-EPMC2527892 | BioStudies
1999-01-01 | S-EPMC22142 | BioStudies
1000-01-01 | S-EPMC2475606 | BioStudies
2006-01-01 | S-EPMC1347986 | BioStudies
1000-01-01 | S-EPMC407822 | BioStudies
2018-01-01 | S-EPMC5951771 | BioStudies
1000-01-01 | S-EPMC3378863 | BioStudies
2011-01-01 | S-EPMC3025773 | BioStudies
2005-01-01 | S-EPMC1183490 | BioStudies