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The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae.

The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae. Research Abstract Details 

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  • The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae. Abstract Text:

    daniel kesslerDaniel Kessler,panagiotis papatheodorouPanagiotis Papatheodorou,tina stratmannTina Stratmann,elke andrea dianElke Andrea Dian,cristina hartmann-fatuCristina Hartmann-Fatu,joachim rassowJoachim Rassow,peter bayerPeter Bayer,jonathan wolf muellerJonathan Wolf Mueller,

    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.

    The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae. Publishing Authors By Initials

    d kesslerD Kessler,p papatheodorouP Papatheodorou,t stratmannT Stratmann,ea dianEA Dian,c hartmann-fatuC Hartmann-Fatu,j rassowJ Rassow,p bayerP Bayer,jw muellerJW Mueller,

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    The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: BMC biology

    VOLUME: 5

    Page Numbers: 37

    Journal Abbreviation: BMC Biol.

    ISSN: 1741-7007

    DAY: 17

    MONTH: 09

    YEAR: 2007

    The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae. Information

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    LANGUAGE: eng

    NlmUniqueID: 101190720

    The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae. Keywords Mesh Terms:

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    Grant and Affiliation Information for The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae.

    AFFILIATION: Department of Structural and Medicinal Biochemistry, Center for Medical Biotechnology - ZMB, University of Duisburg-Essen, 45117 Essen, Germany. daniel.kessler@uni-due.de

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: BMC Biol

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