Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 6-15 |
| Seitenumfang | 10 |
| Fachzeitschrift | Physiologia plantarum |
| Jahrgang | 161 |
| Ausgabenummer | 1 |
| Frühes Online-Datum | 6 März 2017 |
| Publikationsstatus | Veröffentlicht - 17 Aug. 2017 |
Abstract
The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000 kDa and includes 40–50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position. The extra domain includes proteins resembling prokaryotic gamma-type carbonic anhydrases. We here present a detailed comparison of complex I from mammals and flowering plants. Forty homologous subunits are present in complex I of both groups of species. In addition, five subunits are present in mammalian complex I, which are absent in plants, and eight to nine subunits are present in plant complex I which do not occur in mammals. Based on the atomic structure of mammalian complex I and biochemical insights into complex I architecture from plants we mapped the species-specific subunits. Interestingly, four of the five animal-specific and five of the eight to nine plant-specific subunits are localized at the inner surface of the membrane arm of complex I in close proximity. We propose that the inner surface of the membrane arm represents a workbench for attaching proteins to complex I, which are not directly related to respiratory electron transport, like nucleoside kinases, acyl-carrier proteins or carbonic anhydrases. We speculate that further enzyme activities might be bound to this micro-location in other groups of organisms.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Physiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Genetik
- Agrar- und Biowissenschaften (insg.)
- Pflanzenkunde
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: Physiologia plantarum, Jahrgang 161, Nr. 1, 17.08.2017, S. 6-15.
Publikation: Beitrag in Fachzeitschrift › Übersichtsarbeit › Forschung › Peer-Review
}
TY - JOUR
T1 - Structure and function of complex I in animals and plants
T2 - a comparative view
AU - Senkler, Jennifer
AU - Senkler, Michael
AU - Braun, Hans Peter
N1 - Funding information: – This work was supported by the Deutsche Forschungsgemeinschaft (DFG), Forschergruppe 1186 (grant Br1829/10-2).
PY - 2017/8/17
Y1 - 2017/8/17
N2 - The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000 kDa and includes 40–50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position. The extra domain includes proteins resembling prokaryotic gamma-type carbonic anhydrases. We here present a detailed comparison of complex I from mammals and flowering plants. Forty homologous subunits are present in complex I of both groups of species. In addition, five subunits are present in mammalian complex I, which are absent in plants, and eight to nine subunits are present in plant complex I which do not occur in mammals. Based on the atomic structure of mammalian complex I and biochemical insights into complex I architecture from plants we mapped the species-specific subunits. Interestingly, four of the five animal-specific and five of the eight to nine plant-specific subunits are localized at the inner surface of the membrane arm of complex I in close proximity. We propose that the inner surface of the membrane arm represents a workbench for attaching proteins to complex I, which are not directly related to respiratory electron transport, like nucleoside kinases, acyl-carrier proteins or carbonic anhydrases. We speculate that further enzyme activities might be bound to this micro-location in other groups of organisms.
AB - The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000 kDa and includes 40–50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position. The extra domain includes proteins resembling prokaryotic gamma-type carbonic anhydrases. We here present a detailed comparison of complex I from mammals and flowering plants. Forty homologous subunits are present in complex I of both groups of species. In addition, five subunits are present in mammalian complex I, which are absent in plants, and eight to nine subunits are present in plant complex I which do not occur in mammals. Based on the atomic structure of mammalian complex I and biochemical insights into complex I architecture from plants we mapped the species-specific subunits. Interestingly, four of the five animal-specific and five of the eight to nine plant-specific subunits are localized at the inner surface of the membrane arm of complex I in close proximity. We propose that the inner surface of the membrane arm represents a workbench for attaching proteins to complex I, which are not directly related to respiratory electron transport, like nucleoside kinases, acyl-carrier proteins or carbonic anhydrases. We speculate that further enzyme activities might be bound to this micro-location in other groups of organisms.
UR - http://www.scopus.com/inward/record.url?scp=85018971798&partnerID=8YFLogxK
U2 - 10.15488/11654
DO - 10.15488/11654
M3 - Review article
C2 - 28261805
AN - SCOPUS:85018971798
VL - 161
SP - 6
EP - 15
JO - Physiologia plantarum
JF - Physiologia plantarum
SN - 0031-9317
IS - 1
ER -