Characterization of the Overproduced NADH Dehydrogenase Fragment of the NADH:Ubiquinone Oxidoreductase (Complex I) fromEscherichia coli†

Biochemistry ◽  
1998 ◽  
Vol 37 (7) ◽  
pp. 1861-1867 ◽  
Author(s):  
Matthias Braun ◽  
Stefanie Bungert ◽  
Thorsten Friedrich
Keyword(s):  
Complex I ◽  
Nadh Dehydrogenase ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Fromescherichia Coli

Mutants of Chlamydomonas reinhardtii Deficient in Mitochondrial Complex I: Characterization of Two Mutations Affecting the nd1 Coding Sequence

Genetics ◽  
2001 ◽  
Vol 158 (3) ◽  
pp. 1051-1060
Author(s):  
Claire Remacle ◽  
Denis Baurain ◽  
Pierre Cardol ◽  
René F Matagne
Keyword(s):  
Mitochondrial Genome ◽  
Chlamydomonas Reinhardtii ◽  
Complex I ◽  
Slow Growth ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Sequencing Analysis ◽  
Mitochondrial Complex ◽  
Genetical Analysis ◽  
Complex I Activity

Abstract The mitochondrial rotenone-sensitive NADH:ubiquinone oxidoreductase (complex I) comprises more than 30 subunits, the majority of which are encoded by the nucleus. In Chlamydomonas reinhardtii, only five components of complex I are coded for by mitochondrial genes. Three mutants deprived of complex I activity and displaying slow growth in the dark were isolated after mutagenic treatment with acriflavine. A genetical analysis demonstrated that two mutations (dum20 and dum25) affect the mitochondrial genome whereas the third mutation (dn26) is of nuclear origin. Recombinational analyses showed that dum20 and dum25 are closely linked on the genetic map of the mitochondrial genome and could affect the nd1 gene. A sequencing analysis confirmed this conclusion: dum20 is a deletion of one T at codon 243 of nd1; dum25 corresponds to a 6-bp deletion that eliminates two amino acids located in a very conserved hydrophilic segment of the protein.

scholarly journals Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) fromEscherichia coli

2016 ◽  
Vol 160 (4) ◽  
pp. 205-215 ◽  
Author(s):  
Madhavan Narayanan ◽  
Joseph A. Sakyiama ◽  
Mahmoud M. Elguindy ◽  
Eiko Nakamaru-Ogiso
Keyword(s):  
Complex I ◽  
Proton Pumping ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Coupling Mechanism ◽  
Fromescherichia Coli

scholarly journals The mitochondrial AAA protease FTSH3 regulates Complex I abundance by promoting its disassembly

2021 ◽  
Author(s):  
Aneta Ivanova ◽  
Abi S Ghifari ◽  
Oliver Berkowitz ◽  
James Whelan ◽  
Monika W Murcha
Keyword(s):  
Complex I ◽  
Nadh Dehydrogenase ◽  
Slow Growth ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Forward Genetic Screen ◽  
Slow Growth Rate ◽  
Partial Restoration ◽  
Screen Approach

Abstract ATP is generated in mitochondria by oxidative phosphorylation. Complex I (NADH:ubiquinone oxidoreductase or NADH dehydrogenase) is the first multisubunit protein complex of this pathway, oxidising NADH and transferring electrons to the ubiquinone pool. Typically Complex I mutants display a slow growth rate compared to wild-type plants. Here, using a forward genetic screen approach for restored growth of a Complex I mutant, we have identified the mitochondrial ATP dependent metalloprotease, Filamentous Temperature Sensitive H 3 (FTSH3), as a factor that is required for the disassembly of Complex I. An ethyl methanesulfonate-induced mutation in FTSH3, named rmb1 (restoration of mitochondrial biogenesis 1), restored Complex I abundance and plant growth. Complementation could be achieved with FTSH3 lacking proteolytic activity, suggesting the unfoldase function of FTSH3 has a role in Complex I disassembly. The introduction of the rmb1 to an additional, independent, and extensively characterised Complex I mutant, ndufs4, resulted in similar increases to Complex I abundance and a partial restoration of growth. These results show that disassembly or degradation of Complex I plays a role in determining its steady-state abundance and thus turnover may vary under different conditions.

scholarly journals Characterization of a subcomplex of mitochondrial NADH:ubiquinone oxidoreductase (complex I) lacking the flavoprotein part of the N-module

2007 ◽  
Vol 1767 (5) ◽  
pp. 393-400 ◽  
Author(s):  
Volker Zickermann ◽  
Klaus Zwicker ◽  
Maja A. Tocilescu ◽  
Stefan Kerscher ◽  
Ulrich Brandt
Keyword(s):  
Complex I ◽  
Nadh:Ubiquinone Oxidoreductase

scholarly journals Characterization of two novel redox groups in the respiratory NADH:ubiquinone oxidoreductase (complex I)

2000 ◽  
Vol 1459 (2-3) ◽  
pp. 305-309 ◽  
Author(s):  
Thorsten Friedrich ◽  
Benedikt Brors ◽  
Petra Hellwig ◽  
Lars Kintscher ◽  
Tim Rasmussen ◽  
...  
Keyword(s):  
Complex I ◽  
Nadh:Ubiquinone Oxidoreductase

scholarly journals The Campylobacter jejuni NADH:Ubiquinone Oxidoreductase (Complex I) Utilizes Flavodoxin Rather than NADH

2007 ◽  
Vol 190 (3) ◽  
pp. 915-925 ◽  
Author(s):  
Dilan R. Weerakoon ◽  
Jonathan W. Olson
Keyword(s):  
Campylobacter Jejuni ◽  
Complex I ◽  
Nadh Dehydrogenase ◽  
Respiratory Activity ◽  
Essential Gene ◽  
Electron Flow ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
The Novel ◽  
Wild Type ◽  
Transport Chain

ABSTRACT Campylobacter jejuni encodes 12 of the 14 subunits that make up the respiratory enzyme NADH:ubiquinone oxidoreductase (also called complex I). The two nuo genes not present in C. jejuni encode the NADH dehydrogenase, and in their place in the operon are the novel genes designated Cj1575c and Cj1574c. A series of mutants was generated in which each of the 12 nuo genes (homologues to known complex I subunits) was disrupted or deleted. Each of the nuo mutants will not grow in amino acid-based medium unless supplemented with an alternative respiratory substrate such as formate. Unlike the nuo genes, Cj1574c is an essential gene and could not be disrupted unless an intact copy of the gene was provided at an unrelated site on the chromosome. A nuo deletion mutant can efficiently respire formate but is deficient in α-ketoglutarate respiratory activity compared to the wild type. In C. jejuni, α-ketoglutarate respiration is mediated by the enzyme 2-oxoglutarate:acceptor oxidoreductase; mutagenesis of this enzyme abolishes α-ketoglutarate-dependent O2 uptake and fails to reduce the electron transport chain. The electron acceptor for 2-oxoglutarate:acceptor oxidoreductase was determined to be flavodoxin, which was also determined to be an essential protein in C. jejuni. A model is presented in which CJ1574 mediates electron flow into the respiratory transport chain from reduced flavodoxin and through complex I.

Sign in / Sign up

Export Citation Format

Share Document