한빛사 논문
Dong Wook Lee1, Sumin Lee2, Junho Lee2, Seungjin Woo1, Md. Abdur Razzak1, Alessandro Vitale3 and Inhwan Hwang1,2,*
1 Division of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang 37673, Korea
2 Department of Life Sciences, Pohang University of Science and Technology, Pohang 37673, Korea
3 Istituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale Delle Ricerche, Milano, Italy
*Correspondence: Inhwan Hwang
Abstract
Plants possess both types of endosymbiotic organelles, chloroplasts and mitochondria. Transit peptides and presequences function as signal sequences for specific import into chloroplasts and mitochondria, respectively. However, how these highly similar signal sequences confer the protein import specificity remains elusive. Here, we show that mitochondrial- or chloroplast-specific import involves two distinct steps, specificity determination and translocation across envelopes, which are mediated by the N-terminal regions and functionally interchangeable C-terminal regions, respectively, of transit peptides and presequences. A domain harboring multiple-arginine and hydrophobic sequence motifs in the N-terminal regions of presequences was identified as the mitochondrial specificity factor. The presence of this domain and the absence of arginine residues in the N-terminal regions of otherwise common targeting signals confers specificity of protein import into mitochondria and chloroplasts, respectively. AtToc159, a chloroplast import receptor, also contributes to determining chloroplast import specificity. We propose that common ancestral sequences were functionalized into mitochondrial- and chloroplast-specific signal sequences by the presence and absence, respectively, of multiple-arginine and hydrophobic sequence motifs in the N-terminal region.
Key words : transit peptide, presequence, protein import into chloroplasts and mitochondria, N-terminal specificity domain, C-terminal common translocation domain, import specificity determination
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