Nucleotide sequence of the genes coding for α, β and γ subunits of the proton-translocating ATPase of

Kanazawa, Hiroshi; Kayano, Toshiaki; Mabuchi, Kazunori; Futai, Masamitsu

doi:10.1016/0006-291x(81)90494-0

Cited by 108 publications

(31 citation statements)

References 12 publications

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“…The latter, consisting of 43 independent sequences, were FlgBCEFGHIJKL, FlhEAB CD, FliACDSTEFGHIJKLMNOPQR, MotAB, CheAB RWYZ, and a representative receptor, Tar Only one significant similarity was found in these comparisons: Flil showed significant similarity (Fig. 5) to both the 1 and the ax subunits of the ATP-hydrolyzing F1 portion of the FoF1 proton-translocating ATPase from E. coli (26,47,76) and a variety of other cells and organelles, such as Bacillus spp., bovine mitochondria, and maize chloroplasts; F1 13 and a are themselves related (87), although not highly so (26% identity). The optimized scores for the alignments (60) of Flil with F1 1 and a were about 350, while the next nearest scores were about 50 (essentially the noise level).…”

Section: Resultsmentioning

confidence: 99%

Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits

et al. 1991

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Many flagellar proteins are exported by a flagellum-specific export pathway. In an initial attempt to characterize the apparatus responsible for the process, we designed a simple assay to screen for mutants with export defects. Temperature-sensitive flagellar mutants of Salmonella typhimurium were grown at the permissive temperature (30°C), shifted to the restrictive temperature (42°C), and inspected in a light microscope. With the exception of switch mutants, they were fully motile. Next, cells grown at the permissive temperature had their flagellar filaments removed by shearing before the cells were shifted to the restrictive temperature. Most mutants were able to regrow filaments. However, flhA,fliH, fliI, and fiN mutants showed no or greatly reduced regrowth, suggesting that the corresponding gene products are involved in the process of flagellum-specific export. We describe here the sequences offliH,fliI, and the adjacent gene,flij; they encode proteins with deduced molecular masses of 25,782, 49,208, and 17,302 Da, respectively. The deduced sequence of Fliu shows significant similarity to the catalytic 0i subunit of the bacterial FOF, ATPase and to the catalytic subunits of vacuolar and archaebacterial ATPases; except for limited similarity in the motifs that constitute the nucleotide-binding or catalytic site, it appears unrelated to the ElE2 class of ATPases, to other proteins that mediate protein export, or to a variety of other ATP-utilizing enzymes. We hypothesize that FliI is either the catalytic subunit of a protein translocase for flagellum-specific export or a proton translocase involved in local circuits at the flagellum.The bacterial flagellum is a complex structure comprising intracellular, envelope-spanning, and extracellular components. In Salmonella typhimurium, it is encoded by about 40 genes (39).Of those flagellar proteins located within the cell envelope or outside the cell, only the outer-ring (P and L) proteins appear to be exported by the primary signal peptide-dependent pathway (33,36,42). The rest (four rod proteins, a hook protein, three hook-associated proteins, and the filament protein, flagellin) are thought to be exported by a unique, flagellum-specific pathway (30,34,38,59), travelling through the hollow core of the nascent structure (70) and assembling at its distal end (19, 37) (Fig. 1). The process must be a highly organized one, in which protein subunits are incorporated into the growing flagellum in the correct order and stoichiometry (45). The export apparatus obviously must be selective in the proteins it recognizes for export. It may also have to supply energy for the process. Given that the physical path for export is through the nascent structure, it seems likely that the export apparatus is located at the flagellar base (Fig. 1).Essentially nothing is known about this apparatus; specifically, its genetic origin and biochemical composition are completely unknown. We describe here initial attempts to identify its components genetically by use of temperaturesensitive ...

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Section: Resultsmentioning

confidence: 99%

Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits

et al. 1991

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“…Accord- [8,10] and analyzed by SDSjpolyacrylamide gel eleetrophoresis. The order of the genes in the une operon and the eorrelation of genes with A TP-synthase subunits was established genetieally and by nucleotide sequenee analysis [1,[12][13][14][15][16][17][18][19][20][21][22][23]. The numbers below the genes indieate the number of amino acid residues in the subunit polypeptide.…”

Section: Background Problems and Approachesmentioning

confidence: 99%

“…The whole ATP synthase contains, in addition, the five F I subunits IX, ß, y, 8 and E. These eight subunit polypeptides are coded for by the eight genes that form the alp (une) operon (see section IV). The alp operon has been weIl defined geneticaIly, especially by Downie, et al [1,12], and by Von Meyenburg and co-workers [13], and its nucleotide sequence has been determined [14][15][16][17][18][19][20][21][22][23]. Therefore, the subunit composition of the ATP synthase and F o from E. eoli is proven.…”

Section: Background Problems and Approachesmentioning

confidence: 99%

“…The genes of F o preceding the F 1 genes are transcribed in the order a, e, b. The nucleotide sequence has been determined [14][15][16][17][18][19][20][21][22][23] and the sequence has been determined [81][82][83][84]. In yeast, subunit e (proteolipid subunit 9) is encoded on mitochondrial ONA [85], in other organisms in the nucleus [82][83][84][85][86].…”

Section: Iva General Aspectsmentioning

confidence: 99%

“…Ascorbate, a water-soluble agent, did not reduce the signal-generating nitroxide group. From spin-spin interactions between the NCCD moleeules bound to the protein, it was suggested that the pro teins exist in a polymerie form, in whieh some of the monomers are loeated at a maximal distance of [15][16][17][18][19][20] A from each other.…”

Section: Vb Chemical Modificationmentioning

confidence: 99%

See 2 more Smart Citations

The proton conducting F0-part of bacterial ATP synthases

Hoppe¹,

Sebald²

1984

Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics

228

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Energie, Leben und ATP (Nobel-Vortrag)

Boyer

1998

Angewandte Chemie

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Die Zeit genutzt hat Paul Boyer während eines Vortrags, der ihn nicht sonderlich interessierte: Beim Nachdenken über die verwirrenden Ergebnisse von 18O‐Austauschexperimenten erkannte er, daß nicht die Synthese von ATP, sondern hauptsächlich dessen anschließende Freisetzung von der protonenmotorischen Kraft abhängt, die aus den Oxidationsprozessen der Atmungskette stammt – das Konzept des Bindungswechsel‐Mechanismus der ATP‐Synthese war geboren. Für die ATP‐Synthase, die die Bildung von ATP aus ADP und anorganischem Phosphat, eine der wichtigsten Reaktionen in der Natur, katalysiert, fordert dieses Konzept Eigenschaften wie sequentielle Konformationsänderungen und eine diese Änderungen bewirkende Rotation, die dieses Enzym als einzigartige molekulare Maschine erscheinen lassen.

show abstract

Nucleotide sequence of the genes coding for α, β and γ subunits of the proton-translocating ATPase of

Cited by 108 publications

References 12 publications

Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits

Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits

The proton conducting F0-part of bacterial ATP synthases

Energie, Leben und ATP (Nobel-Vortrag)

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