Architecture of the ATP-driven motor for protein import into chloroplasts
Ning Wang, Jiale Xing, Xiaodong Su, Junting Pan, Hui Chen, Lifang Shi, Long Si, Wenqiang Yang, Mei Li
Abstract
Thousands of nuclear-encoded proteins are transported into chloroplasts through the TOC–TIC translocon that spans the chloroplast envelope membranes. A motor complex pulls the translocated proteins out of the TOC–TIC complex into the chloroplast stroma by hydrolyzing ATP. The Orf2971–FtsHi complex has been suggested to serve as the ATP-hydrolyzing motor in Chlamydomonas reinhardtii, but little is known about its architecture and assembly. Here, we report the 3.2-Å resolution structure of the Chlamydomonas Orf2971–FtsHi complex. The 20-subunit complex spans the chloroplast inner envelope, with two bulky modules protruding into the intermembrane space and stromal matrix. Six subunits form a hetero-hexamer that potentially provides the pulling force through ATP hydrolysis. The remaining subunits, including potential enzymes/chaperones, likely facilitate the complex assembly and regulate its proper function. Taken together, our results provide the structural foundation for a mechanistic understanding of chloroplast protein translocation.
附件下载：
Architecture of the ATP-driven motor for protein import into chloroplasts, Mol Plant, 4 Nov 2024
Molecular Plant, 4 November, 2024, DOI：https://doi.org/10.1016/j.molp.2024.09.010
Architecture of the ATP-driven motor for protein import into chloroplasts
Ning Wang, Jiale Xing, Xiaodong Su, Junting Pan, Hui Chen, Lifang Shi, Long Si, Wenqiang Yang, Mei Li
Abstract
Thousands of nuclear-encoded proteins are transported into chloroplasts through the TOC–TIC translocon that spans the chloroplast envelope membranes. A motor complex pulls the translocated proteins out of the TOC–TIC complex into the chloroplast stroma by hydrolyzing ATP. The Orf2971–FtsHi complex has been suggested to serve as the ATP-hydrolyzing motor in Chlamydomonas reinhardtii, but little is known about its architecture and assembly. Here, we report the 3.2-Å resolution structure of the Chlamydomonas Orf2971–FtsHi complex. The 20-subunit complex spans the chloroplast inner envelope, with two bulky modules protruding into the intermembrane space and stromal matrix. Six subunits form a hetero-hexamer that potentially provides the pulling force through ATP hydrolysis. The remaining subunits, including potential enzymes/chaperones, likely facilitate the complex assembly and regulate its proper function. Taken together, our results provide the structural foundation for a mechanistic understanding of chloroplast protein translocation.
文章链接：https://www.sciencedirect.com/science/article/pii/S1674205224002995
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