Kessler, Daniel; Papatheodorou, Panagiotis; Stratmann, Tina; Dian, Elke Andrea; Hartmann-Fatu, Cristina; Rassow, Joachim; Bayer, Peter; Müller, Jonathan W.:
The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae.
In: BMC Biology (incorporating Journal of Biology), Band 5 (2007), S. 37
2007Artikel/Aufsatz in Zeitschrift
BiologieFakultät für Biologie
Damit verbunden: 1 Publikation(en)
Titel in Englisch:
The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae.
Autor*in:
Kessler, Daniel
;
Papatheodorou, Panagiotis
;
Stratmann, TinaUDE
LSF ID
10230
Sonstiges
der Hochschule zugeordnete*r Autor*in
;
Dian, Elke Andrea
;
Hartmann-Fatu, CristinaUDE
LSF ID
10229
Sonstiges
der Hochschule zugeordnete*r Autor*in
;
Rassow, Joachim
;
Bayer, PeterUDE
GND
1059319691
LSF ID
10134
ORCID
0000-0003-0435-7202ORCID iD
Sonstiges
der Hochschule zugeordnete*r Autor*in
;
Müller, Jonathan W.UDE
LSF ID
50179
ORCID
0000-0003-1212-189XORCID iD
Sonstiges
der Hochschule zugeordnete*r Autor*in
Erscheinungsjahr:
2007
PubMed ID
Scopus ID
Sprache des Textes:
Englisch

Abstract in Englisch:

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. © 2007 Kessler et al; licensee BioMed Central Ltd.