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Cross-Species Functional Conservation and Possible Origin of the N-Terminal Specificity Domain of Mitochondrial Presequences

Title
Cross-Species Functional Conservation and Possible Origin of the N-Terminal Specificity Domain of Mitochondrial Presequences
Authors
PARK, SANG KILEE, DON WOOKLee, SuminMin, Chan-KiPark, CanaKIM, JEONG MOKHWANG, CHEOL SANGCho, Nam-HyukHWANG, INHWAN
Date Issued
Feb-2020
Publisher
FRONTIERS MEDIA SA
Abstract
Plants have two endosymbiotic organelles, chloroplast and mitochondrion. Although they have their own genomes, proteome assembly in these organelles depends on the import of proteins encoded by the nuclear genome. Previously, we elucidated the general design principles of chloroplast and mitochondrial targeting signals, transit peptide, and presequence, respectively, which are highly diverse in primary structure. Both targeting signals are composed of N-terminal specificity domain and C-terminal translocation domain. Especially, the N-terminal specificity domain of mitochondrial presequences contains multiple arginine residues and hydrophobic sequence motif. In this study we investigated whether the design principles of plant mitochondrial presequences can be applied to those in other eukaryotic species. We provide evidence that both presequences and import mechanisms are remarkably conserved throughout the species. In addition, we present evidence that the N-terminal specificity domain of presequence might have evolved from the bacterial TAT (twin-arginine translocation) signal sequence.
URI
http://oasis.postech.ac.kr/handle/2014.oak/101355
ISSN
1664-462X
Article Type
Article
Citation
FRONTIERS IN PLANT SCIENCE, vol. 11, 2020-02
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황인환HWANG, INHWAN
Dept of Life Sciences
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