ArticleThe Journal of biological chemistry2015
Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
- Cryo-EM reveals transition states of the Acinetobacter baumannii FFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- Escherichia coli displays a conserved membrane proteomic response to a range of alcohols.Biotechnology for biofuels and bioproducts · 2023Article
- Mechanism of ADP-Inhibited ATP Hydrolysis in Single Proton-Pumping FInternational journal of molecular sciences · 2023Article
- FInternational journal of molecular sciences · 2023Review
- Evolution of the Inhibitory and Non-Inhibitory ε, ζ, and IFMicroorganisms · 2022Review
- Structure of ATP synthase from ESKAPE pathogenScience advances · 2022Article
- Genomewide transcriptional response of Escherichia coli O157:H7 to norepinephrine.BMC genomics · 2022Article
- Regulation of ATP hydrolysis by the ε subunit, ζ subunit and Mg-ADP in the ATP synthase of Paracoccus denitrificans.Biochimica et biophysica acta. Bioenergetics · 2021Article
- Article
- Disrupting coupling within mycobacterial F-ATP synthases subunit ε causes dysregulated energy production and cell wall biosynthesis.Scientific reports · 2019Article
- C-terminal regulatory domain of the ε subunit of FMicrobiologyOpen · 2019Article
- Cryo-EM reveals distinct conformations ofeLife · 2019Article
- ATP synthesis at physiological nucleotide concentrations.Scientific reports · 2019Article
- The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018Review
- Insights into the regulatory function of theOpen biology · 2018Review
- Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.Journal of bioenergetics and biomembranes · 2017Article
- Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
F-type ATP synthases are rotary nanomotor enzymes involved in cellular energy metabolism in eukaryotes and eubacteria. The ATP synthase from Gram-positive and -negative model bacteria can be autoinhibited by the C-terminal domain of its ϵ subunit (ϵCTD), but the importance of ϵ inhibition in vivo is unclear. Functional rotation is thought to be blocked by insertion of the latter half of the ϵCTD into the central cavity of the catalytic complex (F1). In the inhibited state of the Escherichia coli enzyme, the final segment of ϵCTD is deeply buried but has few specific interactions with other subunits. This region of the ϵCTD is variable or absent in other bacteria that exhibit strong ϵ-inhibition in vitro. Here, genetically deleting the last five residues of the ϵCTD (ϵΔ5) caused a greater defect in respiratory growth than did the complete absence of the ϵCTD. Isolated membranes with ϵΔ5 generated proton-motive force by respiration as effectively as with wild-type ϵ but showed a nearly 3-fold decrease in ATP synthesis rate. In contrast, the ϵΔ5 truncation did not change the intrinsic rate of ATP hydrolysis with membranes. Further, the ϵΔ5 subunit retained high affinity for isolated F1 but reduced the maximal inhibition of F1-ATPase by ϵ from >90% to ∼20%. The results suggest that the ϵCTD has distinct regulatory interactions with F1 when rotary catalysis operates in opposite directions for the hydrolysis or synthesis of ATP.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.