An Ankyrin Repeat Domain of AKR2 Drives Chloroplast Targeting through Coincident Binding of Two Chloroplast Lipids
| Autor: | Hwan Su Yoon, Gwang Hyeon Gwon, Seohyeon Song, Antonina Silkov, Eun Chan Yang, Barry Honig, Kyungyoung Song, Dae Heon Kim, Younghyun Kim, Wonhwa Cho, Inhwan Hwang, Zheng Yi Xu, Yunje Cho, Mi Jeong Park |
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| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Chloroplasts Molecular Sequence Data Arabidopsis Plasma protein binding Biology Cyanobacteria General Biochemistry Genetics and Molecular Biology Cytosol Protein structure Amino Acid Sequence Binding site Symbiosis Molecular Biology Peptide sequence Binding Sites Sequence Homology Amino Acid Arabidopsis Proteins Galactolipids Phosphatidylglycerols Cell Biology Chloroplast outer membrane Lipids Ankyrin Repeat Protein Structure Tertiary Chloroplast Biochemistry Ankyrin repeat Function (biology) Molecular Chaperones Protein Binding Developmental Biology |
| Zdroj: | Developmental Cell. 30:598-609 |
| ISSN: | 1534-5807 |
| DOI: | 10.1016/j.devcel.2014.07.026 |
| Popis: | SummaryIn organellogenesis of the chloroplast from endosymbiotic cyanobacteria, the establishment of protein-targeting mechanisms to the chloroplast should have been pivotal. However, it is still mysterious how these mechanisms were established and how they work in plant cells. Here we show that AKR2A, the cytosolic targeting factor for chloroplast outer membrane (COM) proteins, evolved from the ankyrin repeat domain (ARD) of the host cell by stepwise extensions of its N-terminal domain and that two lipids, monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol (PG), of the endosymbiont were selected to function as the AKR2A receptor. Structural analysis, molecular modeling, and mutational analysis of the ARD identified two adjacent sites for coincidental and synergistic binding of MGDG and PG. Based on these findings, we propose that the targeting mechanism of COM proteins was established using components from both the endosymbiont and host cell through a modification of the protein-protein-interacting ARD into a lipid binding domain. |
| Databáze: | OpenAIRE |
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