Assembly of the Cytochrome bo3 Complex

Stenberg, Filippa; Heijne, Gunnar von; Daley, Daniel O.

doi:10.1016/j.jmb.2007.05.045

Cited by 46 publications

(41 citation statements)

References 31 publications

(28 reference statements)

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“…Band 7, detected by heme staining (Fig. 2C), may be attributed to the dimer of cytochrome bo 3 oxygen reductase, previously observed in E. coli intact cells resolved by BN-PAGE [50], due to the proximity of the estimated masses (320 kDa vs. 316 AE 12). This is the first time that it is identified in solubilized membranes, indicating that the solubilization conditions used in this investigation serve to preserve these inter-complex interactions.…”

Section: Detection Of Supercomplexes By Electrophoretic Techniquessupporting

confidence: 52%

Supramolecular organizations in the aerobic respiratory chain of Escherichia coli

et al. 2011

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a b s t r a c tThe organization of respiratory chain complexes in supercomplexes has been shown in the mitochondria of several eukaryotes and in the cell membranes of some bacteria. These supercomplexes are suggested to be important for oxidative phosphorylation efficiency and to prevent the formation of reactive oxygen species.Here we describe, for the first time, the identification of supramolecular organizations in the aerobic respiratory chain of Escherichia coli, including a trimer of succinate dehydrogenase. Furthermore, two heterooligomerizations have been shown: one resulting from the association of the NADH:quinone oxidoreductases NDH-1 and NDH-2, and another composed by the cytochrome bo 3 quinol:oxygen reductase, cytochrome bd quinol:oxygen reductase and formate dehydrogenase (fdo). These results are supported by blue native-electrophoresis, mass spectrometry and kinetic data of wild type and mutant E . coli strains.

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Section: Detection Of Supercomplexes By Electrophoretic Techniquessupporting

confidence: 52%

Supramolecular organizations in the aerobic respiratory chain of Escherichia coli

et al. 2011

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“…One interpretation of these results is that heme a insertion may be necessary for formation or stabilization of the S2 intermediate. In addition, studies of the assembly of the bo 3 oxidase of Escherichia coli revealed that insertion of heme b (analogous to the heme a site in cytochrome oxidase) was necessary for subunit assembly (38).…”

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confidence: 99%

Formation of the Redox Cofactor Centers during Cox1 Maturation in Yeast Cytochrome Oxidase

Khalimonchuk

Bestwick

Meunier

et al. 2010

Molecular and Cellular Biology

126

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“…S1). Taking into account the demonstrated role of the Cpx response in protein folding and degradation and the fact that proper folding of respiratory subunits is required for their assembly into complexes (33), it is possible that in the absence of the Cpx response, respiratory complexes cannot be assembled properly. As little is known about the quality control of membrane-bound respiratory complexes in either mitochondria or E. coli, potential Cpx-regulated factors involved in this process remain mysterious.…”

Section: Discussionmentioning

confidence: 99%

“…Cytochrome bo 3 is a terminal oxidase that couples the oxidation of ubiquinone to the reduction of molecular oxygen. It is composed of four subunits that assemble into a 144-kDa complex within the bacterial IM (29)(30)(31)(32)(33). It is a member of the heme-copper oxidase superfamily that also includes cytochrome c oxidase found in human mitochondria (32,34).…”

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confidence: 99%

A Bacterial Stress Response Regulates Respiratory Protein Complexes To Control Envelope Stress Adaptation

et al. 2017

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The Cpx envelope stress response mediates adaptation to stresses that affect protein folding within the envelope of Gram-negative bacteria. Recent transcriptome analyses revealed that the Cpx response impacts genes that affect multiple cellular functions predominantly associated with the cytoplasmic membrane. In this study, we examined the connection between the Cpx response and the respiratory complexes NADH dehydrogenase I and cytochrome bo 3 in enteropathogenic Escherichia coli. We found that the Cpx response directly represses the transcription of the nuo and cyo operons and that Cpx-mediated repression of these complexes confers adaptation to stresses that compromise envelope integrity. Furthermore, we found that the activity of the aerobic electron transport chain is reduced in E. coli lacking a functional Cpx response despite no change in the transcription of either the nuo or the cyo operon. Finally, we show that expression of NADH dehydrogenase I and cytochrome bo 3 contributes to basal Cpx pathway activity and that overproduction of individual subunits can influence pathway activation. Our results demonstrate that the Cpx response gauges and adjusts the expression, and possibly the function, of inner membrane protein complexes to enable adaptation to envelope stress.IMPORTANCE Bacterial stress responses allow microbes to survive environmental transitions and conditions, such as those encountered during infection and colonization, that would otherwise kill them. Enteric microbes that inhabit or infect the gut are exposed to a plethora of stresses, including changes in pH, nutrient composition, and the presence of other bacteria and toxic compounds. Bacteria detect and adapt to many of these conditions by using envelope stress responses that measure the presence of stressors in the outermost compartment of the bacterium by monitoring its physiology. The Cpx envelope stress response plays a role in antibiotic resistance and host colonization, and we have shown that it regulates many functions at the bacterial inner membrane. In this report, we describe a novel role for the Cpx response in sensing and controlling the expression of large, multiprotein respiratory complexes at the cytoplasmic membrane of Escherichia coli. The significance of our research is that it will increase our understanding of how these stress responses are involved in antibiotic resistance and the mechanisms used by bacteria to colonize the gut.KEYWORDS envelope stress response, NADH dehydrogenase I, cytochrome bo 3 , membrane protein biogenesis, Cpx envelope stress response, NADH dehydrogenase, cytochrome oxidase, inner membrane, protein complex, protein folding, protein localization, respiration, two-component regulatory systems G ram-negative bacteria are characterized by the structure of their cell envelope, which consists of the inner membrane (IM), the outer membrane, and the peptidoglycan layer within the periplasmic space. Of these, the IM contains the greatest protein diversity (1). Proteins that reside within the IM...

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Assembly of the Cytochrome bo3 Complex

Cited by 46 publications

References 31 publications

Supramolecular organizations in the aerobic respiratory chain of Escherichia coli

Supramolecular organizations in the aerobic respiratory chain of Escherichia coli

Formation of the Redox Cofactor Centers during Cox1 Maturation in Yeast Cytochrome Oxidase

A Bacterial Stress Response Regulates Respiratory Protein Complexes To Control Envelope Stress Adaptation

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