Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 405-417 |
| Seitenumfang | 13 |
| Fachzeitschrift | Plant Journal |
| Jahrgang | 98 |
| Ausgabenummer | 3 |
| Frühes Online-Datum | 2 Jan. 2019 |
| Publikationsstatus | Veröffentlicht - 29 Apr. 2019 |
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Genetik
- Agrar- und Biowissenschaften (insg.)
- Pflanzenkunde
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: Plant Journal, Jahrgang 98, Nr. 3, 29.04.2019, S. 405-417.
Publikation: Beitrag in Fachzeitschrift › Übersichtsarbeit › Forschung › Peer-Review
}
TY - JOUR
T1 - Mitochondrial complex II of plants
T2 - subunit composition, assembly, and function in respiration and signaling
AU - Huang, Shaobai
AU - Braun, Hans Peter
AU - Gawryluk, Ryan M.R.
AU - Millar, A. Harvey
N1 - Funding information: SH was funded as an ARC Australian Future Fellow (FT130101338). HPB’s research was supported by the Strategische Fo€rderpro-gramm (SFP) of the Faculty of Natural Sciences/Leibniz Universita€t Hannover. AHM is supported by the Australian Research Council (CE140100008). SH was funded as an ARC Australian Future Fellow (FT130101338). HPB's research was supported by the Strategische F?rderprogramm (SFP) of the Faculty of Natural Sciences/Leibniz Universit?t Hannover. AHM is supported by the Australian Research Council (CE140100008).
PY - 2019/4/29
Y1 - 2019/4/29
N2 - 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.
AB - 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.
KW - assembly factors
KW - complex II
KW - plant mitochondria
KW - reactive oxygen species
KW - stress signaling
KW - succinate dehydrogenase
KW - Reactive Oxygen Species/metabolism
KW - Arabidopsis/metabolism
KW - Mitochondria/metabolism
KW - Succinate Dehydrogenase/metabolism
KW - Nitric Oxide/metabolism
KW - Signal Transduction/physiology
UR - http://www.scopus.com/inward/record.url?scp=85061576941&partnerID=8YFLogxK
U2 - 10.1111/tpj.14227
DO - 10.1111/tpj.14227
M3 - Review article
C2 - 30604579
AN - SCOPUS:85061576941
VL - 98
SP - 405
EP - 417
JO - Plant Journal
JF - Plant Journal
SN - 0960-7412
IS - 3
ER -