Nucleotide sequence of genes coding for dicyclohexylcarbodiimide-binding protein and the α subunit of proton-translocating ATPase of Escherichia coli

Sequence of subunit c of the Na+‐translocating F1FO ATPase of Acetobacterium woodii: proposal for determinants of Na+ specificity as revealed by sequence comparisons

“…2. Alignment of subunit c from A. woodii with subunit c from P. modestum [20], E. hirae [21], E. coli [22], V. alginolyticus [23], thermophilic bacterium PS3 [24], Bacillus megaterium [25], and Synechocystis 6803 [26]. The topology of subunit c is indicated.…”

The proton conducting F0-part of bacterial ATP synthases

“…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.…”

“…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.…”

“…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].…”

“…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.…”