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Structural insights into the coordination of plastid division by the ARC6–PDV2 complex

Nature Plants volume 3, Article number: 17011 (2017) | Download Citation

Abstract

Chloroplasts divide by binary fission, which is accomplished by the simultaneous constriction of the FtsZ ring on the stromal side of the inner envelope membrane, and the ARC5 ring on the cytosolic side of the outer envelope membrane. The two rings are connected and coordinated mainly by the interaction between the inner envelope membrane protein ARC6 and the outer envelope membrane protein PDV2 in the intermembrane space. The underlying mechanism of this coordination is unclear to date. Here, we solved the crystal structure of the intermembrane space region of the ARC6–PDV2 complex. The results indicated that PDV2 inserts its carboxy terminus into a pocket formed in ARC6, and this interaction further induces the dimerization of the intermembrane space regions of two ARC6 molecules. A pdv2 mutant attenuating PDV2-induced ARC6 dimerization showed abnormal morphology of ARC6 rings and compromised chloroplast division in plant cells. Together, our data reveal that PDV2-induced dimerization of ARC6 plays a critical role in chloroplast division and provide insights into the coordination mechanism of the internal and external plastid division machineries.

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Acknowledgements

We would like to thank the staff at beamline BL17U of the Shanghai Synchrotron Radiation Facility for their assistance with data collection, and J. Wang at Tsinghua University for crystallographic data analysis. This work was supported by the National Natural Science Foundation of China (31400635 and 30971439), the Beijing Natural Science Foundation (5154031) and the Fundamental Research Funds for the Central Universities (JD1609).

Author information

Author notes

    • Wenhe Wang
    • , Jinyu Li
    • , Qingqing Sun
    •  & Xiaoyu Yu

    These authors contributed equally to this work.

Affiliations

  1. Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China

    • Wenhe Wang
    • , Xiaoyu Yu
    • , Weiwei Zhang
    • , Yanan Dong
    • , Fengjiao Han
    • , Zhiling Zhu
    • , Shi-zhong Luo
    •  & Yue Feng
  2. College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China

    • Jinyu Li
    • , Qingqing Sun
    • , Ning Jia
    • , Chuanjing An
    • , Yiqiong Li
    • , Ning Chang
    • , Xiaomin Liu
    •  & Hongbo Gao
  3. Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua-Peking Joint Center for Life Sciences, Tsinghua University, Beijing 100084, China

    • You Yu
    • , Shilong Fan
    •  & Maojun Yang

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Contributions

Y.F. and H.G. designed the project. W.W., X.Y., W.Z., Y.D., F.H., Y.Y., S.F., M.Y., N.C., Z.Z. and S.L. purified the proteins, grew the crystals, collected data, solved the crystal structures and performed the in vitro pull-down and gel filtration assays. J.L., N.J., X.L. and N.C. performed the yeast two-hybrid assays. J.L., Q.S., C.A., X.L. and N.C. identified the Arabidopsis mutants, generated transgenic plants and did the microscopy and other analyses. Q.S. and Y.L. performed the immunofluorescence staining experiments. Y.F. analysed the data and wrote the paper with the help of all the authors.

Competing interests

The authors declare no competing financial interests.

Corresponding authors

Correspondence to Hongbo Gao or Yue Feng.

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    Supplementary Information

    Supplementary Methods, Supplementary Figures 1–10, Supplementary Table 1.

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DOI

https://doi.org/10.1038/nplants.2017.11

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