scholarly journals Inhibition of RNase P RNA cleavage by aminoglycosides

1999 ◽  
Vol 96 (11) ◽  
pp. 6155-6160 ◽  
Author(s):  
N. E. Mikkelsen ◽  
M. Brannvall ◽  
A. Virtanen ◽  
L. A. Kirsebom
Keyword(s):  
Rnase P ◽  
2018 ◽  
Vol 52 (6) ◽  
pp. 905-912 ◽  
Author(s):  
D. S. Novopashina ◽  
A. S. Nazarov ◽  
M. A. Vorobjeva ◽  
M. S. Kuprushkin ◽  
A. S. Davydova ◽  
...  

Author(s):  
Arjun Bhatta ◽  
Christian Dienemann ◽  
Patrick Cramer ◽  
Hauke S. Hillen

AbstractHuman mitochondrial transcripts contain messenger and ribosomal RNAs flanked by transfer RNAs (tRNAs), which are excised by mitochondrial RNase (mtRNase) P and Z to liberate all RNA species. In contrast to nuclear or bacterial RNase P, mtRNase P is not a ribozyme but comprises three protein subunits that carry out RNA cleavage and methylation by unknown mechanisms. Here, we present the cryo-EM structure of human mtRNase P bound to precursor tRNA, which reveals a unique mechanism of substrate recognition and processing. Subunits TRMT10C and SDR5C1 form a subcomplex that binds conserved mitochondrial tRNA elements, including the anticodon loop, and positions the tRNA for methylation. The endonuclease PRORP is recruited and activated through interactions with its PPR and nuclease domains to ensure precise pre-tRNA cleavage. The structure provides the molecular basis for the first step of RNA processing in human mitochondria.


1995 ◽  
Vol 247 (2) ◽  
pp. 161-172 ◽  
Author(s):  
Wolf-Dietrich Hardt ◽  
Judith Schlegl ◽  
Volker A. Erdmann ◽  
Roland K. Hartmann

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Anthony Gobert ◽  
Yifat Quan ◽  
Mathilde Arrivé ◽  
Florent Waltz ◽  
Nathalie Da Silva ◽  
...  

AbstractPlant viruses cause massive crop yield loss worldwide. Most plant viruses are RNA viruses, many of which contain a functional tRNA-like structure. RNase P has the enzymatic activity to catalyze the 5′ maturation of precursor tRNAs. It is also able to cleave tRNA-like structures. However, RNase P enzymes only accumulate in the nucleus, mitochondria, and chloroplasts rather than cytosol where virus replication takes place. Here, we report a biotechnology strategy based on the re-localization of plant protein-only RNase P to the cytosol (CytoRP) to target plant viruses tRNA-like structures and thus hamper virus replication. We demonstrate the cytosol localization of protein-only RNase P in Arabidopsis protoplasts. In addition, we provide in vitro evidences for CytoRP to cleave turnip yellow mosaic virus and oilseed rape mosaic virus. However, we observe varied in vivo results. The possible reasons have been discussed. Overall, the results provided here show the potential of using CytoRP for combating some plant viral diseases.


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