ArticleBMC biology2007
The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae.
Article in BMC biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- The Actin-Binding Prolyl-Isomerase Par17 Sustains Its Substrate Selectivity by Interdomain Allostery.Proteins · 2025Article
- Expression, Purification, Structural and Functional Characterization of Recombinant Human Parvulin 17.Molecular biotechnology · 2023Article
- Review
- PIN1 and PIN4 inhibitionFrontiers in microbiology · 2023Article
- A Redox-Sensitive Cysteine Is Required for PIN1At Function.Frontiers in plant science · 2021Article
- Parvulin 14 and Parvulin 17 Bind to HBx and cccDNA and Upregulate Hepatitis B Virus Replication from cccDNA to Virion in an HBx-Dependent Manner.Journal of virology · 2019Article
- Human DHEA sulfation requires direct interaction between PAPS synthase 2 and DHEA sulfotransferase SULT2A1.The Journal of biological chemistry · 2018Article
- Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.Journal of medicinal chemistry · 2016Review
- NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase.BMC biology · 2016Article
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner.The Journal of biological chemistry · 2015Article
- Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.Biomolecules · 2015Review
- Human DNA-binding peptidyl-prolyl cis/trans isomerase Par14 is cell cycle dependently expressed and associates with chromatin in vivo.BMC biochemistry · 2015Article
- ShaPINg Cell Fate Upon DNA Damage: Role of Pin1 Isomerase in DNA Damage-Induced Cell Death and Repair.Frontiers in oncology · 2014Review
- The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Biochimica et biophysica acta · 2014Review
- Human PAPS synthase isoforms are dynamically regulated enzymes with access to nucleus and cytoplasm.PloS one · 2012Article
- Structure and dynamics of the first archaeal parvulin reveal a new functionally important loop in parvulin-type prolyl isomerases.The Journal of biological chemistry · 2011Article
- Single-domain parvulins constitute a specific marker for recently proposed deep-branching archaeal subgroups.Evolutionary bioinformatics online · 2011Article
- Small family with key contacts: par14 and par17 parvulin proteins, relatives of pin1, now emerge in biomedical research.Perspectives in medicinal chemistry · 2008Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe 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.
resultsBased 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.
conclusionTaken 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.
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