ArticleThe Journal of biological chemistry2013
Subunit δ is the key player for assembly of the H(+)-translocating unit of Escherichia coli F(O)F1 ATP synthase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- CGL160-mediated recruitment of the coupling factor CF1 is required for efficient thylakoid ATP synthase assembly, photosynthesis, and chloroplast development in Arabidopsis.The Plant cell · 2023Article
- Gene crosstalk between COVID-19 and preeclampsia revealed by blood transcriptome analysis.Frontiers in immunology · 2023Article
- ATP5D Is a Potential Biomarker for Male Fertility.Oxidative medicine and cellular longevity · 2023Article
- Subunits E-F-G of E. coli Complex I can form an active complex when expressed alone, but in time-delayed assembly co-expression of B-CD-E-F-G is optimal.Biochimica et biophysica acta. Bioenergetics · 2022Article
- Low membrane fluidity triggers lipid phase separation and protein segregation in living bacteria.The EMBO journal · 2022Article
- Analysis of the assembly pathway for membrane subunits of Complex I reveals that subunit L (ND5) can assemble last inBBA advances · 2021Article
- The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018Review
- Two separate modules of the conserved regulatory RNA AbcR1 address multiple target mRNAs in and outside of the translation initiation region.RNA biology · 2014Article
- Time-delayed in vivo assembly of subunit a into preformed Escherichia coli FoF1 ATP synthase.Journal of bacteriology · 2013Article
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7 authors.
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Abstract
The ATP synthase (F(O)F1) of Escherichia coli couples the translocation of protons across the cytoplasmic membrane to the synthesis or hydrolysis of ATP. This nanomotor is composed of the rotor c10γε and the stator ab2α3β3δ. To study the assembly of this multimeric enzyme complex consisting of membrane-integral as well as peripheral hydrophilic subunits, we combined nearest neighbor analyses by intermolecular disulfide bond formation or purification of partially assembled F(O)F1 complexes by affinity chromatography with the use of mutants synthesizing different sets of F(O)F1 subunits. Together with a time-delayed in vivo assembly system, the results demonstrate that F(O)F1 is assembled in a modular way via subcomplexes, thereby preventing the formation of a functional H(+)-translocating unit as intermediate product. Surprisingly, during the biogenesis of F(O)F1, F1 subunit δ is the key player in generating stable F(O). Subunit δ serves as clamp between ab2 and c10α3β3γε and guarantees that the open H(+) channel is concomitantly assembled within coupled F(O)F1 to maintain the low membrane proton permeability essential for viability, a general prerequisite for the assembly of multimeric H(+)-translocating enzymes.
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