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- W2041844964 abstract "Abstract Unlike most previously characterized mitochondrial coupling factors, F 1 -ATPases, the enzyme purified from etiolated pea ( Pisum sativum L.) contains six subunits. The additional subunit designated as δ′ has an apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of 23 000 and was detected by immunoblotting. Both genomic and partial cDNA clones encoding the δ′-subunit have been isolated and sequenced. The 591 bp coding region deduced from the cDNA and genomic sequences encoded a 197 amino acid precursor protein with a calculated molecular weight of 21 274. Untranslated 5′ and 3′ regions of 132 and 177 bp, respectively, were also determined. The N-terminus of the precursor protein contained a 19 amino acid presequence homologous to signal peptides for mitochondrial targeting. The mature protein is comprised of 178 residues with a molecular weight of 18 758. The mature δ′-subunit shows 73% identity at the amino acid level with the sweet potato δ′-subunit and marked homology with the N-terminal protein sequence of the turnip δ′-subunit. Comparison of the δ′-subunit of pea with other organisms indicated that its counterparts are the δ-subunit of bovine and fungal F 1 and the ϵ-subunit of bacterial F 1 and chloroplast CF 1 . The subunit identified as δ from pea mitochondrial F 1 is the oligomycin-sensitivity-conferring protein." @default.
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- W2041844964 date "1993-01-01" @default.
- W2041844964 modified "2023-09-27" @default.
- W2041844964 title "Cloning the δ′-subunit of the mitochondrial F1-ATPase from peas" @default.
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- W2041844964 doi "https://doi.org/10.1016/0168-9452(93)90138-p" @default.
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