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Succinate:quinone oxidoreductases

Succinat:Quinon-Oxidoreduktasen
Authors: Karavaeva, Valeriya;

Succinate:quinone oxidoreductases

Abstract

Succinatdehydrogenasen (SDHs) und Fumaratreduktasen (FRDs) katalysieren die gegenseitige Umwandlung von Succinat und Fumarat. Komplex II steht seit vielen Jahren im Mittelpunkt der Forschung, da diese Reaktion in allen Domänen des Lebens hochgradig konserviert ist, die katalytischen Untereinheiten dieses Komplexes homolog zu einer Vielzahl anderer Proteine sind, und diese Enzyme ein Teil von den (an)aeroben Elektronentransportketten und dem Citratzyklus sind. Die aktuelle Klassifikation von SDH/FRDs basiert auf der Struktur von Membrananker-Untereinheiten und ihren Cofaktoren. Die Forschung von Komplex II wurde jedoch im Zusammenhang mit der Evolution oder der taxonomischen Verbreitung nicht umfassend analysiert. In dieser Arbeit befasst sich eine groß angelegte vergleichende Genomanalyse von Komplex II mit den Fragen der taxonomischen Verteilung und Phylogenie. Unsere Ergebnisse zeigen, dass für die Typen C, D und F strukturelle Klassifizierung und Phylogenie Hand in Hand gehen, während die Situation für die Typen A, B und E komplexer ist, was die Möglichkeit ihrer Klassifizierung in Untergruppen hervorhebt. Basierend auf diesen Erkenntnissen wird ein neues Evolutionsszenario für diese Enzyme vorgeschlagen, in dem ein primordiales lösliches Modul, das den zytoplasmatischen Untereinheiten entspricht, die aktuelle Diversität über mehrere unabhängige Membrananker-Anheftungsereignisse hervorrufen würde. Die Ergebnisse dieses Projekts betonen auch die Notwendigkeit einer weiteren biochemischen Charakterisierung von taxonomisch diversen SDH/FRDs verschiedener Typen, die derzeit fehlt.

Succinate dehydrogenases (SDHs) and fumarate reductases (FRDs) catalyze the interconversion of succinate and fumarate. Complex II has been a focus of research for many years because this reaction is highly conserved in all domains of life, the cytoplasmic subunits of this complex are homologous to a variety of other proteins, and the enzymes are part of (an)aerobic electron transport chains and the TCA cycle. The current classification of SDH/FRDs is based on the structure of membrane anchor subunits and their cofactors. However, complex II has not been widely analyzed in the context of evolution or taxonomic distribution. In this work, a large-scale comparative genomics analysis of complex II addresses the questions of taxonomic distribution and phylogeny. Our findings report that for types C, D, and F, the structural classification and phylogeny go hand in hand, while for types A, B and E the situation is more complex, highlighting the possibility for their classification into subgroups. Based on these findings, a new evolutionary scenario is proposed, in which a primordial soluble module, corresponding to the cytoplasmic subunits, would give rise to the current diversity via several independent membrane anchor attachment events. The results of this project also emphasize the necessity of further biochemical characterization of taxonomically diverse SDH/FRDs of different types, which is currently lacking.

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
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