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Updated: Jul 11, 2026

Genotyping Single Nucleotide Polymorphisms in the Mitochondrial Genome by Pyrosequencing
Published on: February 10, 2023
The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely
Daniel Kessler1, Panagiotis Papatheodorou, Tina Stratmann
1Department of Structural and Medicinal Biochemistry, Center for Medical Biotechnology - ZMB, University of Duisburg-Essen, 45117 Essen, Germany. daniel.kessler@uni-due.de
Background:
The parvulin-type peptidyl prolyl cis/trans isomerase Par14 is highly conserved in all metazoans. The recently identified parvulin Par17 contains an additional N-terminal domain whose occurrence and function was the focus of the present study.
Results:
Based on the observation that the human genome encodes Par17, but bovine and rodent genomes do not, Par17 exon sequences from 10 different primate species were cloned and sequenced. Par17 is encoded in the genomes of Hominidae species including humans, but is absent from other mammalian species. In contrast to Par14, endogenous Par17 was found in mitochondrial and membrane fractions of human cell lysates. Fluorescence of EGFP fusions of Par17, but not Par14, co-localized with mitochondrial staining. Par14 and Par17 associated with isolated human, rat and yeast mitochondria at low salt concentrations, but only the Par17 mitochondrial association was resistant to higher salt concentrations. Par17 was imported into mitochondria in a time and membrane potential-dependent manner, where it reached the mitochondrial matrix. Moreover, Par17 was shown to bind to double-stranded DNA under physiological salt conditions.
Conclusion:
Taken together, the DNA binding parvulin Par17 is targeted to the mitochondrial matrix by the most recently evolved mitochondrial prepeptide known to date, thus adding a novel protein constituent to the mitochondrial proteome of Hominidae.
Insights
The newly discovered parvulin Par17, found in humans but not other mammals, targets the mitochondrial matrix. This DNA-binding protein represents a novel component of the human mitochondrial proteome.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Parvulin-type peptidyl prolyl cis/trans isomerase Par14 is highly conserved across metazoans.
- The recently identified parvulin Par17 possesses a unique N-terminal domain, prompting investigation into its evolutionary occurrence and functional role.
Purpose of the Study:
- To investigate the evolutionary presence and subcellular localization of parvulin Par17.
- To determine the functional characteristics of Par17, including its mitochondrial targeting and DNA-binding capabilities.
Main Methods:
- Genomic analysis of Par17 exon sequences across 10 primate species.
- Subcellular fractionation and immunofluorescence microscopy of human cell lysates.
- Mitochondrial import assays and DNA-binding assays under varying salt conditions.
Main Results:
- Par17 is encoded in Hominidae genomes (including humans) but absent in other mammalian species studied.
- Endogenous Par17 localizes to mitochondria and membrane fractions, with EGFP fusions co-localizing with mitochondrial markers.
- Par17 exhibits salt-resistant association with mitochondria, is imported into the mitochondrial matrix dependent on membrane potential, and binds double-stranded DNA.
Conclusions:
- Parvulin Par17 is a DNA-binding protein specifically targeted to the mitochondrial matrix.
- Its mitochondrial targeting is mediated by a recently evolved mitochondrial prepeptide.
- Par17 represents a novel protein constituent of the Hominidae mitochondrial proteome.
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