Escherichia coli F1Fo-ATP Synthase with a b/δ Fusion Protein Allows Analysis of the Function of the Individual b Subunits

Gajadeera, Chathurada S.; Weber, Joachim

doi:10.1074/jbc.m113.503722

Cited by 13 publications

(9 citation statements)

References 44 publications

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“…Subunit b¢ is packed tightly against the second and third transmembrane a helices of subunit a while subunit b-d forms fewer contacts. These interactions explain the observation that subunit b-d is responsible for mediating attachment with the F1 region while subunit b¢ is more important for binding the FO region (Gajadeera and Weber, 2013). The d region of the b-d fusion subunit differs dramatically from the canonical bacterial ATP synthase d subunit (Fig.…”

Section: Overall Structure Of Mycobacterial Atp Synthase Includes An mentioning

confidence: 84%

Structure of mycobacterial ATP synthase with the TB drug bedaquiline

Guo

Courbon

Bueler

et al. 2020

Preprint

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SummaryTuberculosis (TB), the leading cause of death by infectious disease worldwide, is increasingly resistant to first line antibiotics. Developed from a screen against Mycobacterium smegmatis, bedaquiline can sterilize even latent M. tuberculosis infections that may otherwise persist for decades and has become a cornerstone of treatment for multidrug resistant and extensively-drug resistant TB. Bedaquiline targets mycobacterial ATP synthase, an essential enzyme in the obligate aerobic Mycobacterium genus. However, how the drug binds the intact enzyme is unknown. We determined the structure of M. smegmatis ATP synthase with and without bedaquiline. The drug-free structure reveals hook-like extensions from the enzyme’s α subunits that inhibit ATP hydrolysis in low-energy conditions, such as during latent infections. Bedaquiline binding induces global conformational changes in ATP synthase, creating tight binding pockets at the interface of subunits a and c. These binding sites explain the drug’s structure-activity relationship and its potency as an antibiotic for TB.

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Section: Overall Structure Of Mycobacterial Atp Synthase Includes An mentioning

confidence: 84%

Structure of mycobacterial ATP synthase with the TB drug bedaquiline

Guo

Courbon

Bueler

et al. 2020

Preprint

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“…The rps and rpl genes encode the small and large subunits of ribosomal proteins, and splicing deficiency of rps and rpl genes affects ribosome biogenesis and assembly (Schmitz-Linneweber et al, 2006;Asakura et al, 2012;Chi et al, 2012). The atpF is a subunit of proton-transporting ATP synthase complex that catalyzes the final step of oxidative phosphorylation and photophosphorylation (Gajadeera and Weber, 2013). It is likely that decreased levels of rps12, rpl21, and atpF transcripts caused by splicing deficiency in AtRH3 mutants affect ribosome biogenesis and ATP synthesis, which results in retarded growth of the mutant plants under normal and stress conditions.…”

Section: Discussionmentioning

confidence: 99%

“…The roles of RHs in the metabolism of aberrant and silencing RNAs during the regulation of mRNA quality control and gene expression in plant development have been demonstrated (reviewed in Linder and Owttrim, 2009). The functional roles of several RHs have also been demonstrated in the stress responses of plants (Gong et al, 2005;Kant et al, 2007;Kim et al, 2008;Li et al, 2008).…”

Section: Introductionmentioning

confidence: 97%

A chloroplast-localized DEAD-box RNA helicaseAtRH3 is essential for intron splicing and plays an important role in the growth and stress response in Arabidopsis thaliana

Lee

et al. 2014

Plant Physiology and Biochemistry

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“…A recent study of the ATPV complex showed that such paralogous expansions can lead to increased complexity (and possibly also specificity) of a multi-subunit molecular machine [42] . Moreover, ATPF0B functions as a dimer, even in species where only one copy exists in the genome, and the two parts of the dimer interact with different parts of the F 1 and the F 0 subcomplex [43] , [44] . Thus a gene duplication which allows each gene copy to fine-tune specific interactions may indeed be advantageous.…”

Section: Discussionmentioning

confidence: 99%

Evolution of the F0F1 ATP Synthase Complex in Light of the Patchy Distribution of Different Bioenergetic Pathways across Prokaryotes

Koumandou

Κοσσίδα

2014

PLoS Comput Biol

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Bacteria and archaea are characterized by an amazing metabolic diversity, which allows them to persist in diverse and often extreme habitats. Apart from oxygenic photosynthesis and oxidative phosphorylation, well-studied processes from chloroplasts and mitochondria of plants and animals, prokaryotes utilize various chemo- or lithotrophic modes, such as anoxygenic photosynthesis, iron oxidation and reduction, sulfate reduction, and methanogenesis. Most bioenergetic pathways have a similar general structure, with an electron transport chain composed of protein complexes acting as electron donors and acceptors, as well as a central cytochrome complex, mobile electron carriers, and an ATP synthase. While each pathway has been studied in considerable detail in isolation, not much is known about their relative evolutionary relationships. Wanting to address how this metabolic diversity evolved, we mapped the distribution of nine bioenergetic modes on a phylogenetic tree based on 16S rRNA sequences from 272 species representing the full diversity of prokaryotic lineages. This highlights the patchy distribution of many pathways across different lineages, and suggests either up to 26 independent origins or 17 horizontal gene transfer events. Next, we used comparative genomics and phylogenetic analysis of all subunits of the F0F1 ATP synthase, common to most bacterial lineages regardless of their bioenergetic mode. Our results indicate an ancient origin of this protein complex, and no clustering based on bioenergetic mode, which suggests that no special modifications are needed for the ATP synthase to work with different electron transport chains. Moreover, examination of the ATP synthase genetic locus indicates various gene rearrangements in the different bacterial lineages, ancient duplications of atpI and of the beta subunit of the F0 subcomplex, as well as more recent stochastic lineage-specific and species-specific duplications of all subunits. We discuss the implications of the overall pattern of conservation and flexibility of the F0F1 ATP synthase genetic locus.

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Escherichia coli F1Fo-ATP Synthase with a b/δ Fusion Protein Allows Analysis of the Function of the Individual b Subunits

Cited by 13 publications

References 44 publications

Structure of mycobacterial ATP synthase with the TB drug bedaquiline

Structure of mycobacterial ATP synthase with the TB drug bedaquiline

A chloroplast-localized DEAD-box RNA helicaseAtRH3 is essential for intron splicing and plays an important role in the growth and stress response in Arabidopsis thaliana

Evolution of the F0F1 ATP Synthase Complex in Light of the Patchy Distribution of Different Bioenergetic Pathways across Prokaryotes

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