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Updated: Jun 23, 2026

Discrimintion and Mapping of the Primary and Processed Transcripts in Maize Mitochondrion Using a Circular RT-PCR-based Strategy
Published on: July 29, 2019
tRNA recognition, processing, and disease: hypotheses around an unorthodox type of RNase P in human mitochondria
Johann Holzmann1, Walter Rossmanith
1Center for Anatomy and Cell Biology, Medical University of Vienna, Währinger Strasse 13, 1090 Vienna, Austria.
Abstract:
RNase P is the endonuclease responsible for the maturation of the 5' ends of tRNAs. A catalytic RNA component was long considered the premier attribute of the enzyme family. Ignoring this heritage, human mitochondria make their RNase P of three proteins only. While one of them appears to be the metallonuclease actually responsible for phosphodiester hydrolysis, the other two have been recruited from unrelated biochemical pathways and may be critical for substrate recognition. One of them is moreover identical to a previously identified amyloid-beta-binding protein, whereby it could link tRNA processing to mitochondrial dysfunction in Alzheimer's disease.
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