Guide DNA technique in bacterial ribonuclease P reaction for effective processing of tRNA precursor

2002 ◽  
Vol 36 (2) ◽  
pp. 85
Author(s):  
Terumichi Tanaka ◽  
Yoshiaki Hori ◽  
Yo Kikuchi
Author(s):  
Yoshiaki Hori ◽  
Maria C. Rogert ◽  
Terumichi Tanaka ◽  
Yo Kikuchi ◽  
Elena V. Bichenkova ◽  
...  
Keyword(s):  

Nature ◽  
2003 ◽  
Vol 421 (6924) ◽  
pp. 760-764 ◽  
Author(s):  
Andrey S. Krasilnikov ◽  
Xiaojing Yang ◽  
Tao Pan ◽  
Alfonso Mondragón

Biochemistry ◽  
1994 ◽  
Vol 33 (35) ◽  
pp. 10800-10808 ◽  
Author(s):  
Daniel N. Frank ◽  
Michael E. Harris ◽  
Norman R. Pace

FEBS Letters ◽  
2001 ◽  
Vol 491 (1-2) ◽  
pp. 94-98 ◽  
Author(s):  
Terumichi Tanaka ◽  
Hideo Baba ◽  
Yoshiaki Hori ◽  
Yo Kikuchi

RNA ◽  
2022 ◽  
pp. rna.078814.121
Author(s):  
Anna Ender ◽  
Nadine Grafl ◽  
Tim Kolberg ◽  
Sven Findeiss ◽  
Peter F. Stadler ◽  
...  

Removal of the 5' leader region is an essential step in the maturation of tRNA molecules in all domains of life. This reaction is catalyzed by various RNase P activities, ranging from ribonucleoproteins with ribozyme activity to protein-only forms. In Escherichia coli, the efficiency of RNase P mediated cleavage can be controlled by computationally designed riboswitch elements in a ligand-dependent way, where the 5' leader sequence of a tRNA precursor is either sequestered in a hairpin structure or presented as a single-stranded region accessible for maturation. In the presented work, the regulatory potential of such artificial constructs is tested on different forms of eukaryotic RNase P enzymes – two protein-only RNase P enzymes (PRORP1 and PRORP2) from Arabidopsis thaliana and the ribonucleoprotein of Homo sapiens. The PRORP enzymes were analyzed in vitro as well as in vivo in a bacterial RNase P complementation system. We also tested in HEK293T cells whether the riboswitches remain functional with human nuclear RNase P. While the regulatory principle of the synthetic riboswitches applies for all tested RNase P enzymes, the results also show differences in the substrate requirements of the individual enzyme versions. Hence, such designed RNase P riboswitches represent a novel tool to investigate the impact of the structural composition of the 5'-leader on substrate recognition by different types of RNase P enzymes.


Sign in / Sign up

Export Citation Format

Share Document