The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present
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BioMed Central
Open Access
Research article
The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae Daniel Kessler†1, Panagiotis Papatheodorou†2, Tina Stratmann1, Elke Andrea Dian2, Cristina Hartmann-Fatu1, Joachim Rassow2, Peter Bayer*1 and Jonathan Wolf Mueller*1 Address: 1Department of Structural and Medicinal Biochemistry, Center for Medical Biotechnology – ZMB, University of Duisburg-Essen, 45117 Essen, Germany and 2Institut für Physiologische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany Email: Daniel Kessler - [email protected]; Panagiotis Papatheodorou - [email protected]; Tina Stratmann - [email protected]; Elke Andrea Dian - [email protected]; Cristina Hartmann-Fatu - [email protected]; Joachim Rassow - [email protected]; Peter Bayer* - [email protected]; Jonathan Wolf Mueller* - [email protected] * Corresponding authors †Equal contributors
Published: 17 September 2007 BMC Biology 2007, 5:37
doi:10.1186/1741-7007-5-37
Received: 16 February 2007 Accepted: 17 September 2007
This article is available from: http://www.biomedcentral.com/1741-7007/5/37 © 2007 Kessler et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract 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.
Background Peptidyl prolyl cis/trans isomerases (PPIases, EC 5.2.1
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