High molecular weight forms of mammalian respiratory chain complex II.

Mitochondrial respiratory chain is organised into supramolecular structures that can be preserved in mild detergent solubilisates and resolved by native electrophoretic systems. Supercomplexes of respiratory complexes I, III and IV as well as multimeric forms of ATP synthase are well established. Ho...

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Autores principales:	Nikola Kovářová, Tomáš Mráček, Hana Nůsková, Eliška Holzerová, Marek Vrbacký, Petr Pecina, Kateřina Hejzlarová, Katarína Kľučková, Jakub Rohlena, Jiri Neuzil, Josef Houštěk
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/76d0d12defb74322a7150c596dcb1190
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spelling	oai:doaj.org-article:76d0d12defb74322a7150c596dcb11902021-11-18T08:59:50ZHigh molecular weight forms of mammalian respiratory chain complex II.1932-620310.1371/journal.pone.0071869https://doaj.org/article/76d0d12defb74322a7150c596dcb11902013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23967256/?tool=EBIhttps://doaj.org/toc/1932-6203Mitochondrial respiratory chain is organised into supramolecular structures that can be preserved in mild detergent solubilisates and resolved by native electrophoretic systems. Supercomplexes of respiratory complexes I, III and IV as well as multimeric forms of ATP synthase are well established. However, the involvement of complex II, linking respiratory chain with tricarboxylic acid cycle, in mitochondrial supercomplexes is questionable. Here we show that digitonin-solubilised complex II quantitatively forms high molecular weight structures (CIIhmw) that can be resolved by clear native electrophoresis. CIIhmw structures are enzymatically active and differ in electrophoretic mobility between tissues (500 - over 1000 kDa) and cultured cells (400-670 kDa). While their formation is unaffected by isolated defects in other respiratory chain complexes, they are destabilised in mtDNA-depleted, rho0 cells. Molecular interactions responsible for the assembly of CIIhmw are rather weak with the complexes being more stable in tissues than in cultured cells. While electrophoretic studies and immunoprecipitation experiments of CIIhmw do not indicate specific interactions with the respiratory chain complexes I, III or IV or enzymes of the tricarboxylic acid cycle, they point out to a specific interaction between CII and ATP synthase.Nikola KovářováTomáš MráčekHana NůskováEliška HolzerováMarek VrbackýPetr PecinaKateřina HejzlarováKatarína KľučkováJakub RohlenaJiri NeuzilJosef HouštěkPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e71869 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nikola Kovářová Tomáš Mráček Hana Nůsková Eliška Holzerová Marek Vrbacký Petr Pecina Kateřina Hejzlarová Katarína Kľučková Jakub Rohlena Jiri Neuzil Josef Houštěk High molecular weight forms of mammalian respiratory chain complex II.
description	Mitochondrial respiratory chain is organised into supramolecular structures that can be preserved in mild detergent solubilisates and resolved by native electrophoretic systems. Supercomplexes of respiratory complexes I, III and IV as well as multimeric forms of ATP synthase are well established. However, the involvement of complex II, linking respiratory chain with tricarboxylic acid cycle, in mitochondrial supercomplexes is questionable. Here we show that digitonin-solubilised complex II quantitatively forms high molecular weight structures (CIIhmw) that can be resolved by clear native electrophoresis. CIIhmw structures are enzymatically active and differ in electrophoretic mobility between tissues (500 - over 1000 kDa) and cultured cells (400-670 kDa). While their formation is unaffected by isolated defects in other respiratory chain complexes, they are destabilised in mtDNA-depleted, rho0 cells. Molecular interactions responsible for the assembly of CIIhmw are rather weak with the complexes being more stable in tissues than in cultured cells. While electrophoretic studies and immunoprecipitation experiments of CIIhmw do not indicate specific interactions with the respiratory chain complexes I, III or IV or enzymes of the tricarboxylic acid cycle, they point out to a specific interaction between CII and ATP synthase.
format	article
author	Nikola Kovářová Tomáš Mráček Hana Nůsková Eliška Holzerová Marek Vrbacký Petr Pecina Kateřina Hejzlarová Katarína Kľučková Jakub Rohlena Jiri Neuzil Josef Houštěk
author_facet	Nikola Kovářová Tomáš Mráček Hana Nůsková Eliška Holzerová Marek Vrbacký Petr Pecina Kateřina Hejzlarová Katarína Kľučková Jakub Rohlena Jiri Neuzil Josef Houštěk
author_sort	Nikola Kovářová
title	High molecular weight forms of mammalian respiratory chain complex II.
title_short	High molecular weight forms of mammalian respiratory chain complex II.
title_full	High molecular weight forms of mammalian respiratory chain complex II.
title_fullStr	High molecular weight forms of mammalian respiratory chain complex II.
title_full_unstemmed	High molecular weight forms of mammalian respiratory chain complex II.
title_sort	high molecular weight forms of mammalian respiratory chain complex ii.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/76d0d12defb74322a7150c596dcb1190
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High molecular weight forms of mammalian respiratory chain complex II.

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