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The nuclear‐encoded polypeptide Cfo‐II from spinach is a real, ninth subunit of chloroplast ATP synthase
Author(s) -
Herrmann Reinhold G.,
Steppuhn Johannes,
Herrmann Gernot S.,
Nelson Nathan
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81789-3
Subject(s) - atp synthase gamma subunit , atp synthase , chloroplast , protein subunit , biology , thylakoid , biochemistry , transit peptide , plastid , chloroplast dna , microbiology and biotechnology , atpase , gene , enzyme , atp hydrolysis
Proton‐translocating F‐ATP synthases from chloroplasts contain a nuclear‐coded subunit, CFo‐II, that lacks an equivalent in the corresponding E. coli complex. Three recombinant phages that code for the entire precursor of this subunit have been isolated from λ gt11 cDNA expression libraries made from polyadenylated spinach RNA using a two‐step strategy. The reading frame of 222 amino acid residues includes 147 residues for the mature protein ( M r 16.5 kDa) and a transit sequence of 75 residues ( M r 8.0 kDa). Secondary structure predictions indicate a bitopic protein, anchored by a single N‐terminal transmembrane segment and a C‐terminal hydrophilic region that probably reaches into CF 1 . CFo‐II precursor made in vitro can be imported into isolated, intact chloroplasts and assembled into ATP synthase. This protein is a real subunit of the plastid enzyme and a distinctive characteristic of ATP synthases involved in photosynthetic processes. Unique features are (i) that the gene for CFo‐II ( atp G) appears to be a duplication of atp F encoding CFo‐I, the homologues of the genes for subunits b ′ and b in photosynthetic bacteria, (ii) that it represents the first instance that one copy of the various duplicated loci found in plastid chromosomes has been phylogenetically translocated to the nucleus, and (iii) that it operates with a bipartite (import/thylakoid‐targeting) transit peptide but without an intermediate cleavage site for the stroma protease, suggestive of a way of membrane integration different from that of its plastome‐encoded counterpart CFo‐I. With these data, the first complete sequence for a chloroplast ATP synthase of a higher plant (spinach) is available.