scholarly journals Disease-associated mutations in mitochondrial precursor tRNAs affect binding, m1R9 methylation and tRNA processing by mtRNase P

RNA ◽  
2020 ◽  
pp. rna.077198.120
Author(s):  
Agnes Karasik ◽  
Catherine A. Wilhelm ◽  
Carol A. Fierke ◽  
Markos Koutmos
Keyword(s):  
1988 ◽  
Vol 8 (12) ◽  
pp. 5140-5149
Author(s):  
S S Wang ◽  
A K Hopper

To identify genes involved in pre-tRNA processing, we searched for yeast DNA sequences that specifically enhanced the expression of the SUP4(G37) gene. The SUP4(G37) gene possesses a point mutation at position 37 of suppressor tRNA(Tyr). This lesion results in a reduced rate of pre-tRNA splicing and a decreased level of nonsense suppression. A SUP4(G37) strain was transformed with a yeast genomic library, and the transformants were screened for increased suppressor activity. One transformant contained a plasmid that encoded an unessential gene, STP1, that in multiple copies enhanced the suppression of SUP4(G37) and caused increased production of mature SUP4(G37) product. Disruption of the genomic copy of STP1 resulted in a reduced efficiency of SUP4-mediated suppression and the accumulation of pre-tRNAs. Not all intron-containing pre-tRNAs were affected by the stp1-disruption. At least five of the nine families of pre-tRNAs were affected. Two other species, pre-tRNA(Ile) and pre-tRNA(3Leu), were not. We propose that STP1 encodes a tRNA species-specific product that functions as a helper for pre-tRNA splicing. The STP1 product may interact with pre-tRNAs to generate a structure that is efficiently recognized by splicing machinery.


FEBS Letters ◽  
2009 ◽  
Vol 584 (2) ◽  
pp. 287-296 ◽  
Author(s):  
Lien B. Lai ◽  
Agustín Vioque ◽  
Leif A. Kirsebom ◽  
Venkat Gopalan

tRNA ◽  
2014 ◽  
pp. 51-65 ◽  
Author(s):  
Murray P. Deutscher
Keyword(s):  

2017 ◽  
Vol 114 (42) ◽  
pp. 11121-11126 ◽  
Author(s):  
Astrid I. Nickel ◽  
Nadine B. Wäber ◽  
Markus Gößringer ◽  
Marcus Lechner ◽  
Uwe Linne ◽  
...  

RNase P is an essential tRNA-processing enzyme in all domains of life. We identified an unknown type of protein-only RNase P in the hyperthermophilic bacterium Aquifex aeolicus: Without an RNA subunit and the smallest of its kind, the 23-kDa polypeptide comprises a metallonuclease domain only. The protein has RNase P activity in vitro and rescued the growth of Escherichia coli and Saccharomyces cerevisiae strains with inactivations of their more complex and larger endogenous ribonucleoprotein RNase P. Homologs of Aquifex RNase P (HARP) were identified in many Archaea and some Bacteria, of which all Archaea and most Bacteria also encode an RNA-based RNase P; activity of both RNase P forms from the same bacterium or archaeon could be verified in two selected cases. Bioinformatic analyses suggest that A. aeolicus and related Aquificaceae likely acquired HARP by horizontal gene transfer from an archaeon.


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