한빛사논문
Junho Lee 1#, Byeongho Moon 1#, Dong Wook Lee 2,3, Inhwan Hwang 1*
1Department of Life Science, Pohang University of Science and Technology, Pohang, 790-784, South Korea.
2Department of Integrative Food, Bioscience and Biotechnology, Chonnam National University, Gwangju, 61186, South Korea.
3Department Bioenergy Science and Technology, Chonnam National University, Gwangju, 61186, South Korea.
#These two authors contributed equally to this work.: Junho Lee, Byeongho Moon
*CORRESPONDING AUTHOR : Inhwan Hwang
Abstract
Protein biogenesis is a complex process, and complexity is greatly increased in eukaryotic cells through specific targeting of proteins to different organelles. To direct targeting, organellar proteins carry an organelle-specific targeting signal for recognition by organelle-specific import machinery. However, the situation is confusing for transmembrane domain (TMD)-containing signal-anchored (SA) proteins of various organelles because TMDs function as an endoplasmic reticulum (ER) targeting signal. Although ER targeting of SA proteins is well understood, how they are targeted to mitochondria and chloroplasts remains elusive. Here, we investigated how the targeting specificity of SA proteins is determined for specific targeting to mitochondria and chloroplasts. Mitochondrial targeting requires multiple motifs around and within TMDs: a basic residue and an arginine-rich region flanking the N- and C-termini of TMDs, respectively, and an aromatic residue in the C-terminal side of the TMD that specify mitochondrial targeting in an additive manner. These motifs play a role in slowing down the elongation speed during translation, thereby ensuring mitochondrial targeting in a co-translational manner. By contrast, the absence of any of these motifs individually or together causes at varying degrees chloroplast targeting that occurs in a post-translational manner.
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