Nucleotide sequence of the gene coding for the δ subunit of proton-translocating ATPase of Escherichia coli

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Abstract

The DNA sequence of a part of the gene cluster for the proton-translocating ATPase of E. coli was determined. Two reading frames were found between the genes for dicyclohexylcarbodiimide-binding protein and α subunit. The following evidence indicates that one frame codes the δ subunit; i) The primary structure deduced from DNA sequence agreed with amino acid composition of the protein. ii) Five residues from the amino terminal were the same as those deduced from DNA sequence. The α helix content of this protein (estimated from the primary structure) was 60.2% of the total residues with the longest helical domain of 50 residues. The intercistronic sequence between the genes for δ and α had 15 base pairs, suggesting that the synthesis of the α is not regulated transcriptionally. The organization of the gene cluster was also shown on the physical map.

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    Abbreviations: H+-ATPase, proton-translocating ATPase; F1, peripheral membrane component of H+-ATPase; F0, intrinsic membrane component of H+-ATPase; DCCD, N′-dicyclohexylacrbodiimide; N, N′-dicyclohexylacrbodiimide; DCCD-binding protein, a subunit of F0 capable of binding DCCD; α, β, γ, δ, and ϵ, five subunits of F1. 24K, 18K, 19K and 14K indicate polypeptides with apparent molecular weights of 24,000, 18,000, 19,000 and 14,000 daltons, respectively. As discussed in the text 18K and 19K may be the same component in F0, and the slight difference of the molecular weights may be within experimental errors in calibrating molecular weights.

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    Copyright © 1981 Published by Elsevier Inc.