H+-ATPase of Escherichia coli. An uncE mutation impairing coupling between F1 and Fo but not Fo-mediated H+ translocation.

Mosher, M E; White, Laura K.; Hermolin, Joe; Fillingame, Robert H.

doi:10.1016/s0021-9258(18)89143-8

Cited by 84 publications

(12 citation statements)

References 22 publications

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“…Second, the overexpression of the mutant form of the homolog in Drosophila resulted in statistically significant impairment of mobility (geotaxis), whereas that of wild‐type protein did not. Third, as a naturally occurring mutation, p.N102E, in the homologous E. coli gene, atpE reduces complex V function and ATP production (while preserving proton translocation) 7 . We studied this mutation and found that both Drosophila geotaxis and complex V activity were significantly reduced, although to a lesser extent than with the human mutation.…”

Section: Discussionmentioning

confidence: 96%

“…Third, as a naturally occurring mutation, p.N102E, in the homologous E. coli gene, atpE reduces complex V function and ATP production (while preserving proton translocation). 7 We studied this mutation and found that both Drosophila geotaxis and complex V activity were significantly reduced, although to a lesser extent than with the human mutation. Finally, the human mutation reduced complex V activity in Drosophila with a severity that matched that observed motor slowing in the geotaxis assays.…”

Section: Discussionmentioning

confidence: 97%

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A Novel Variant of ATP5MC3 Associated with Both Dystonia and Spastic Paraplegia

et al. 2021

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Background In a large pedigree with an unusual phenotype of spastic paraplegia or dystonia and autosomal dominant inheritance, linkage analysis previously mapped the disease to chromosome 2q24‐2q31. Objective The aim of this study is to identify the genetic cause and molecular basis of an unusual autosomal dominant spastic paraplegia and dystonia. Methods Whole exome sequencing following linkage analysis was used to identify the genetic cause in a large family. Cosegregation analysis was also performed. An additional 384 individuals with spastic paraplegia or dystonia were screened for pathogenic sequence variants in the adenosine triphosphate (ATP) synthase membrane subunit C locus 3 gene (ATP5MC3). The identified variant was submitted to the “GeneMatcher” program for recruitment of additional subjects. Mitochondrial functions were analyzed in patient‐derived fibroblast cell lines. Transgenic Drosophila carrying mutants were studied for movement behavior and mitochondrial function. Results Exome analysis revealed a variant (c.318C > G; p.Asn106Lys) (NM_001689.4) in ATP5MC3 in a large family with autosomal dominant spastic paraplegia and dystonia that cosegregated with affected individuals. No variants were identified in an additional 384 individuals with spastic paraplegia or dystonia. GeneMatcher identified an individual with the same genetic change, acquired de novo, who manifested upper‐limb dystonia. Patient fibroblast studies showed impaired complex V activity, ATP generation, and oxygen consumption. Drosophila carrying orthologous mutations also exhibited impaired mitochondrial function and displayed reduced mobility. Conclusion A unique form of familial spastic paraplegia and dystonia is associated with a heterozygous ATP5MC3 variant that also reduces mitochondrial complex V activity.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 97%

A Novel Variant of ATP5MC3 Associated with Both Dystonia and Spastic Paraplegia

et al. 2021

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“…

been shown to disrupt the binding and functional coupling of F] to F0 (Mosher et al, 1985;Miller et al, 1989), and the simplest explanation is to place these residues at the F0-F] interface. This interpretation is supported by the experiments presented here, where an epitope in the Lys34 -* * Ile^segment of the protein was placed at the Frbinding surface of the membrane.

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confidence: 99%

Folding of a peptide corresponding to the .alpha.-helix in bovine pancreatic trypsin inhibitor

Goodman

Kim²

1989

Biochemistry

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A short peptide corresponding to the alpha-helical region of BPTI shows partial folding in aqueous solution (pH 7) as judged by circular dichroism (CD). Folding is temperature and denaturant sensitive, and the peptide is monomeric. The difference CD spectrum, obtained from spectra at two temperatures, indicates that the peptide folds as an alpha-helix. Difference CD spectroscopy provides a sensitive assay for helix formation in peptides exhibiting small amounts of structure. Helix stability in this peptide shows a marked pH dependence which is consistent with stabilizing charged side-chain interactions with the helix dipole and/or salt bridge formation.

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“…Only Tyr73 was reducible by treatment of right-side-out membrane vesicles with sodium dithionite, and this observation places the C-terminus of the protein at the outside surface of the membrane. been shown to disrupt the binding and functional coupling of F] to F0 (Mosher et al, 1985;Miller et al, 1989), and the simplest explanation is to place these residues at the F0-F] interface. This interpretation is supported by the experiments presented here, where an epitope in the Lys34 -* * Ile^segment of the protein was placed at the Fj-binding surface of the membrane.…”

Section: Discussionmentioning

confidence: 99%

“…Loo and Bragg (1982) prepared antiserum to purified subunit c and demonstrated that it blocked binding of F, to the F0 exposed in Frstripped membranes, but the epitopes recognized by the antiserum were not defined. We have proposed that the evolutionarily invariant Arg41-Gln42-Pro43 sequence of the polar loop plays a critical role in coupling H+ translocation through F0 to ATP synthesis in Fb based upon the properties of mutants in this sequence (Mosher et al, 1985;Miller et al, 1989). In this study we have addressed the question of whether the polar loop sequence extends from the F, binding inner surface of the E. coli inner membrane and conclude that it does.…”

mentioning

confidence: 94%

Organization of the F0 sector of Escherichia coli proton-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membrane

Girvin¹,

Hermolin²,

Pottorf³

et al. 1989

Biochemistry

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The membrane-spanning F0 sector of the Escherichia coli H+-transporting ATP synthase (EC 3.6.1.34) contains multiple copies of subunit c, a 79 amino acid residue protein that is thought to insert in the membrane like a hairpin with two membrane traversing alpha-helices. The center of the protein is much more polar than the putative transmembrane alpha-helices and has been postulated to play a crucial role in coupling H+ translocation through F0 to ATP synthesis in the membrane extrinsic, F1 sector of the complex. However, the direction of insertion of subunit c in the membrane has not been established. We show here that the "polar loop" lies on the F1 binding side of the membrane. A peptide corresponding to Lys34----Ile46 of the polar loop was synthesized. Antisera were generated to the Lys34----Ile46 cognate peptide, and the polyclonal antipeptide IgG was shown to bind to a crude F0 fraction by using enzyme-linked immunosorbent assays. The antipeptide serum did not bind tightly enough to F0 to disrupt function. However, a polyclonal antiserum made to purified, whole subunit c was shown to block the binding of F1 to the F0 exposed in F1-stripped membranes. Incubation of the antisubunit c serum with the peptide reduced the inhibitory effect of the antiserum on the binding of F1 to F0. The reversal of inhibition by the peptide was specific to the antisubunit c serum in that the peptide had no effect on inhibition of F1 binding to F0 by antiserum to subunit a of F0.(ABSTRACT TRUNCATED AT 250 WORDS)

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H+-ATPase of Escherichia coli. An uncE mutation impairing coupling between F1 and Fo but not Fo-mediated H+ translocation.

Cited by 84 publications

References 22 publications

A Novel Variant of ATP5MC3 Associated with Both Dystonia and Spastic Paraplegia

A Novel Variant of ATP5MC3 Associated with Both Dystonia and Spastic Paraplegia

Folding of a peptide corresponding to the .alpha.-helix in bovine pancreatic trypsin inhibitor

Organization of the F0 sector of Escherichia coli proton-ATPase: the polar loop region of subunit c extends from the cytoplasmic face of the membrane

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