Abstract：
:In 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.
journal_name
Dev Celljournal_title
Developmental cellauthors
Kim DH,Park MJ,Gwon GH,Silkov A,Xu ZY,Yang EC,Song S,Song K,Kim Y,Yoon HS,Honig B,Cho W,Cho Y,Hwang Idoi
10.1016/j.devcel.2014.07.026subject
Has Abstractpub_date
2014-09-08 00:00:00pages
598-609issue
5eissn
1534-5807issn
1878-1551pii
S1534-5807(14)00492-4journal_volume
30pub_type
杂志文章abstract：:Exposing cells to folding stress causes a subset of their proteins to misfold and accumulate in inclusion bodies (IBs). IB formation and clearance are both active processes, but little is known about their mechanism. To shed light on this issue, we performed a screen with over 4,000 fluorescently tagged yeast proteins...
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journal_title：Developmental cell
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journal_title：Developmental cell
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journal_title：Developmental cell
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journal_title：Developmental cell
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