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MBE Advance Access originally published online on April 22, 2009
Molecular Biology and Evolution 2009 26(8):1773-1780; doi:10.1093/molbev/msp087
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© The Author 2009. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Research Articles

Diversity in Degrees of Freedom of Mitochondrial Transit Peptides

Christine Staiger*,{dagger},1,2, Alexander Hinneburg*,2 and Ralf Bernd Klösgen{dagger}

* Faculty of Science III, Institute of Computer Science, Martin-Luther-University Halle-Wittenberg, Halle/Saale, Germany
{dagger} Faculty of Science I, Institute of Biology—Plant Physiology, Martin Luther University Halle-Wittenberg, Germany

E-mail: klosgen{at}pflanzenphys.uni-halle.de.

Accepted for publication April 14, 2009.

Most mitochondrial proteins are synthesized in the cytosol of eukaryotic cells as precursor proteins carrying N-terminal extensions called transit peptides or presequences, which mediate their specific transport into mitochondria. However, plant cells possess a second potential target organelle for such transit peptides, the chloroplast. It can therefore be assumed that mitochondrial transit peptides in plants are exposed to an increased demand of specificity, which in turn leads to reduced degrees of freedom in these transit peptides compared with those of nonplant organisms. Our study investigates this hypothesis using fractal dimension. Statistical analysis of sequence data shows that the fractal dimension of mitochondrial transit peptides in plants is indeed significantly lower than that from nonplant organisms.

Key Words: mitochondria • transit peptide • degrees of freedom • fractal dimension • target organelle • organelle specificity

1 Present address: BioSystems Research Group, School of Computing, University of Leeds, Leeds, United Kingdom.

2 Both authors contributed equally to this work.

Martin Embley, Associate Editor


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