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  1. Article ; Online: Disordered-to-ordered transitions in assembly factors allow the complex II catalytic subunit to switch binding partners.

    Sharma, Pankaj / Maklashina, Elena / Voehler, Markus / Balintova, Sona / Dvorakova, Sarka / Kraus, Michal / Hadrava Vanova, Katerina / Nahacka, Zuzana / Zobalova, Renata / Boukalova, Stepana / Cunatova, Kristyna / Mracek, Tomas / Ghayee, Hans K / Pacak, Karel / Rohlena, Jakub / Neuzil, Jiri / Cecchini, Gary / Iverson, T M

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 473

    Abstract: Complex II (CII) activity controls phenomena that require crosstalk between metabolism and signaling, including neurodegeneration, cancer metabolism, immune activation, and ischemia-reperfusion injury. CII activity can be regulated at the level of ... ...

    Abstract Complex II (CII) activity controls phenomena that require crosstalk between metabolism and signaling, including neurodegeneration, cancer metabolism, immune activation, and ischemia-reperfusion injury. CII activity can be regulated at the level of assembly, a process that leverages metastable assembly intermediates. The nature of these intermediates and how CII subunits transfer between metastable complexes remains unclear. In this work, we identify metastable species containing the SDHA subunit and its assembly factors, and we assign a preferred temporal sequence of appearance of these species during CII assembly. Structures of two species show that the assembly factors undergo disordered-to-ordered transitions without the appearance of significant secondary structure. The findings identify that intrinsically disordered regions are critical in regulating CII assembly, an observation that has implications for the control of assembly in other biomolecular complexes.
    MeSH term(s) Catalytic Domain ; Protein Structure, Secondary
    Language English
    Publishing date 2024-01-11
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-44563-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Residual Complex I activity and amphidirectional Complex II operation support glutamate catabolism through mtSLP in anoxia.

    Ravasz, Dora / Bui, David / Nazarian, Sara / Pallag, Gergely / Karnok, Noemi / Roberts, Jennie / Marzullo, Bryan P / Tennant, Daniel A / Greenwood, Bennett / Kitayev, Alex / Hill, Collin / Komlódi, Timea / Doerrier, Carolina / Cunatova, Kristyna / Fernandez-Vizarra, Erika / Gnaiger, Erich / Kiebish, Michael A / Raska, Alexandra / Kolev, Krasimir /
    Czumbel, Bence / Narain, Niven R / Seyfried, Thomas N / Chinopoulos, Christos

    Scientific reports

    2024  Volume 14, Issue 1, Page(s) 1729

    Abstract: Anoxia halts oxidative phosphorylation (OXPHOS) causing an accumulation of reduced compounds in the mitochondrial matrix which impedes dehydrogenases. By simultaneously measuring oxygen concentration, NADH autofluorescence, mitochondrial membrane ... ...

    Abstract Anoxia halts oxidative phosphorylation (OXPHOS) causing an accumulation of reduced compounds in the mitochondrial matrix which impedes dehydrogenases. By simultaneously measuring oxygen concentration, NADH autofluorescence, mitochondrial membrane potential and ubiquinone reduction extent in isolated mitochondria in real-time, we demonstrate that Complex I utilized endogenous quinones to oxidize NADH under acute anoxia.
    MeSH term(s) Humans ; NAD/metabolism ; Mitochondria/metabolism ; Electron Transport Complex I/metabolism ; Quinones/metabolism ; Oxidative Phosphorylation ; Succinates/metabolism ; Hypoxia/metabolism ; Oxidation-Reduction
    Chemical Substances NAD (0U46U6E8UK) ; Electron Transport Complex I (EC 7.1.1.2) ; Quinones ; Succinates
    Language English
    Publishing date 2024-01-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-024-51365-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Cytochrome

    Pajuelo Reguera, David / Čunátová, Kristýna / Vrbacký, Marek / Pecinová, Alena / Houštěk, Josef / Mráček, Tomáš / Pecina, Petr

    Cells

    2020  Volume 9, Issue 2

    Abstract: ... ...

    Abstract Cytochrome
    MeSH term(s) Cytochromes c/metabolism ; Gene Expression Regulation, Enzymologic/physiology ; HEK293 Cells ; Humans ; Oxygen/metabolism ; Protein Isoforms/metabolism
    Chemical Substances Protein Isoforms ; Cytochromes c (9007-43-6) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2020-02-14
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells9020443
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Loss of COX4I1 Leads to Combined Respiratory Chain Deficiency and Impaired Mitochondrial Protein Synthesis.

    Čunátová, Kristýna / Reguera, David Pajuelo / Vrbacký, Marek / Fernández-Vizarra, Erika / Ding, Shujing / Fearnley, Ian M / Zeviani, Massimo / Houštěk, Josef / Mráček, Tomáš / Pecina, Petr

    Cells

    2021  Volume 10, Issue 2

    Abstract: The oxidative phosphorylation (OXPHOS) system localized in the inner mitochondrial membrane secures production of the majority of ATP in mammalian organisms. Individual OXPHOS complexes form supramolecular assemblies termed supercomplexes. The complexes ... ...

    Abstract The oxidative phosphorylation (OXPHOS) system localized in the inner mitochondrial membrane secures production of the majority of ATP in mammalian organisms. Individual OXPHOS complexes form supramolecular assemblies termed supercomplexes. The complexes are linked not only by their function but also by interdependency of individual complex biogenesis or maintenance. For instance, cytochrome
    MeSH term(s) Electron Transport Complex IV/metabolism ; Glycolysis ; HEK293 Cells ; Humans ; Mitochondrial Diseases/metabolism ; Mitochondrial Proteins/biosynthesis ; Oxidative Phosphorylation ; Oxygen Consumption ; Protein Biosynthesis ; Protein Subunits/metabolism
    Chemical Substances Mitochondrial Proteins ; Protein Subunits ; COX4I1 protein, human (EC 1.9.3.1) ; Electron Transport Complex IV (EC 1.9.3.1)
    Language English
    Publishing date 2021-02-10
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells10020369
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: TMEM70 facilitates biogenesis of mammalian ATP synthase by promoting subunit c incorporation into the rotor structure of the enzyme.

    Kovalčíkova, Jana / Vrbacký, Marek / Pecina, Petr / Tauchmannová, Kateřina / Nůsková, Hana / Kaplanová, Vilma / Brázdová, Andrea / Alán, Lukáš / Eliáš, Jan / Čunátová, Kristýna / Kořínek, Vladimír / Sedlacek, Radislav / Mráček, Tomáš / Houštěk, Josef

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2019  Volume 33, Issue 12, Page(s) 14103–14117

    Abstract: Biogenesis of ... ...

    Abstract Biogenesis of F
    MeSH term(s) Animals ; Cells, Cultured ; Gene Expression Regulation ; Gene Knockout Techniques/methods ; Genotype ; HEK293 Cells ; Humans ; Mice ; Mice, Knockout ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitochondrial Proton-Translocating ATPases/genetics ; Mitochondrial Proton-Translocating ATPases/metabolism ; Proteolipids/metabolism ; Tamoxifen/pharmacology
    Chemical Substances Mitochondrial Proteins ; Proteolipids ; Tamoxifen (094ZI81Y45) ; Mitochondrial Proton-Translocating ATPases (EC 3.6.3.-)
    Language English
    Publishing date 2019-10-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.201900685RR
    Database MEDical Literature Analysis and Retrieval System OnLINE

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