Supramolecular assembly of chloroplast NADH dehydrogenase-like complex with photosystem I from Arabidopsis thaliana

Xiaodong Su; Duanfang Cao; Xiaowei Pan; Lifang Shi; Zhenfeng Liu; Luca Dall'Osto; Roberto Bassi; Xinzheng Zhang; Mei Li

doi:10.1016/j.molp.2022.01.020

Supramolecular assembly of chloroplast NADH dehydrogenase-like complex with photosystem I from Arabidopsis thaliana

Mol Plant. 2022 Mar 7;15(3):454-467. doi: 10.1016/j.molp.2022.01.020. Epub 2022 Feb 2.

Authors

Xiaodong Su¹, Duanfang Cao², Xiaowei Pan³, Lifang Shi², Zhenfeng Liu¹, Luca Dall'Osto⁴, Roberto Bassi⁴, Xinzheng Zhang⁵, Mei Li⁶

Affiliations

¹ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China; University of Chinese Academy of Sciences, Beijing 100049, P.R. China.
² National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China.
³ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China; College of Life Science, Capital Normal University, Beijing 100101, P.R. China. Electronic address: panxw@cnu.edu.cn.
⁴ Dipartimento di Biotecnologie, Università di Verona, 37134 Verona, Italy.
⁵ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China; University of Chinese Academy of Sciences, Beijing 100049, P.R. China; Center for Biological Imaging, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China. Electronic address: xzzhang@ibp.ac.cn.
⁶ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China. Electronic address: meili@ibp.ac.cn.

PMID: 35123031
DOI: 10.1016/j.molp.2022.01.020

Abstract

Cyclic electron transport/flow (CET/CEF) in chloroplasts is a regulatory process essential for the optimization of plant photosynthetic efficiency. A crucial CEF pathway is catalyzed by a membrane-embedded NADH dehydrogenase-like (NDH) complex that contains at least 29 protein subunits and associates with photosystem I (PSI) to form the NDH-PSI supercomplex. Here, we report the 3.9 Å resolution structure of the Arabidopsis thaliana NDH-PSI (AtNDH-PSI) supercomplex. We constructed structural models for 26 AtNDH subunits, among which 11 are unique to chloroplasts and stabilize the core part of the NDH complex. In the supercomplex, one NDH can bind up to two PSI-light-harvesting complex I (PSI-LHCI) complexes at both sides of its membrane arm. Two minor LHCIs, Lhca5 and Lhca6, each present in one PSI-LHCI, interact with NDH and contribute to supercomplex formation and stabilization. Collectively, our study reveals the structural details of the AtNDH-PSI supercomplex assembly and provides a molecular basis for further investigation of the regulatory mechanism of CEF in plants.

Keywords: Arabidopsis thaliana; NADH dehydrogenase-like (NDH) complex; cyclic electron transport/flow; photosystem I; structure.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Arabidopsis Proteins* / metabolism
Arabidopsis* / metabolism
Chloroplasts / metabolism
Light-Harvesting Protein Complexes / metabolism
NADH Dehydrogenase / metabolism
Photosystem I Protein Complex / metabolism

Substances

Arabidopsis Proteins
Light-Harvesting Protein Complexes
Photosystem I Protein Complex
NADH Dehydrogenase