Mitochondrial complex II of plants: subunit composition, assembly, and function in respiration and signaling

Shaobai Huang, Hans-Peter Braun, Ryan Gawryluk, Andrew Millar

Research output: Contribution to journalReview article

9 Citations (Scopus)

Abstract

Complex II [succinate dehydrogenase (succinate-ubiquinone oxidoreductase); EC 1.3.5.1; SDH] is the only enzyme shared by both the electron transport chain and the tricarboxylic acid (TCA) cycle in mitochondria. Complex II in plants is considered unusual because of its accessory subunits (SDH5-SDH8), in addition to the catalytic subunits of SDH found in all eukaryotes (SDH1-SDH4). Here, we review compositional and phylogenetic analysis and biochemical dissection studies to both clarify the presence and propose a role for these subunits. We also consider the wider functional and phylogenetic evidence for SDH assembly factors and the reports from plants on the control of SDH1 flavination and SDH1-SDH2 interaction. Plant complex II has been shown to influence stomatal opening, the plant defense response and reactive oxygen species-dependent stress responses. Signaling molecules such as salicyclic acid (SA) and nitric oxide (NO) are also reported to interact with the ubiquinone (UQ) binding site of SDH, influencing signaling transduction in plants. Future directions for SDH research in plants and the specific roles of its different subunits and assembly factors are suggested, including the potential for reverse electron transport to explain the succinate-dependent production of reactive oxygen species in plants and new avenues to explore the evolution of plant mitochondrial complex II and its utility.

Significance Statement Mitochondrial complex II is the only component shared between the electron transport chain and the tricarboxylic acid (TCA) cycle, and it plays a key role in respiration, metabolism and signaling in stress and pathogen responses in plants.

Original languageEnglish
Pages (from-to)405-417
Number of pages13
JournalThe Plant Journal
Volume98
Issue number3
DOIs
Publication statusPublished - May 2019

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