The chloroplast genes encoding subunits of the H+-ATP synthase

Hudson, Graham S.; Mason, John G.

doi:10.1007/bf00042985

Cited by 31 publications

(15 citation statements)

References 86 publications

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“…It has been concluded, that subunit Fob and CFoI are identical in secondary structure, topographical location and function in the diverse ATP-synthase complexes [1,2,6,8,9]. In the case of E. coli the topography has been analyzed with biochemical methods, antibodies, proteases, crosslinking and labels (for review see [20]).…”

Section: Production and Analysis Of Antisera Againstmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…CFo contains four different polypeptides [l-3]; subunits IV, I and III are chloroplast encoded and sequenced [ 1,2], polypeptide II is nuclear encoded, imported as a precursor [4] and partially sequenced [S]. Homologies in sequence and hydropathy suggest that subunit CFOIV corresponds to Foa, CFOI to Fob and CF0111 to FOC of the E. coli ATPase [ 1,2]. The hydropathy analysis indicates one membrane span and an extension of the protein into an aqueous space for CFOI [6]; thus it would be suitable to build part of the 'stalk', but no biochemical results support this notion until now for chloroplasts.…”

Section: Introductionmentioning

confidence: 99%

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Quantitative immunochemical evidence for identical topography of subunits CF₀II and CF₀I within the photosynthetic ATP‐synthase of spinach chloroplasts

Otto

Berzborn

1989

FEBS Letters

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Monospecific polyclonal antisera against the 16 kDa and the 18 kDa polypeptides II and I from the CF, moiety of the photosynthetic ATP-synthase in spinach were produced. Inhibition, agglutination and absorption experiments were combined with quantitative determinations in ELISA of residual antibodies and of amounts of CF, and CF,. It follows that subunits CF,II and CF,,I are membrane anchored, extend into the matrix space, and are partially shielded underneath or within CF,. These results on the structure suggest that CF,II and CF,,I are homologous to each other, and in function both homologous to E. coli F,b; thus CF,,II together with CF,I would be part of the 'stalk'.

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Section: Production and Analysis Of Antisera Againstmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Quantitative immunochemical evidence for identical topography of subunits CF₀II and CF₀I within the photosynthetic ATP‐synthase of spinach chloroplasts

Otto

Berzborn

1989

FEBS Letters

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“…ATPase, EC 3.6.1.34) are multimeric enzyme complexes of the cytoplasmic membrane of eubacteria [l], the inner membrane of mitochondria, and the thylakoid membrane of cyanobacteria and chloroplasts [2,3]. Characterization by DNA sequence analysis of the genes has demonstrated that many features of their structures are conserved [4].…”

Section: Introduction Fofi-atpases (Proton-translocatingmentioning

confidence: 99%

The primary structure of the γ‐subunit of the ATPase from Synechocystis 6803

1990

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The nucleotide sequence of the gene coding for the F,F,-ATPase y-subunit (arpC) from the transformable cyanobacterium Synechocystis 6083 has been determined. The deduced translation product consists of 314 amino acid residues and is highly homologous (72% identical residues) to the sequences of other cyanobacterial y-subunits. The Synechocystis 6803 sequence is also homologous to the chloroplast y-sequence. Like in the other cyanobacterial subunits, only the first of the 3 cysteine residues, which are involved in energy-linked functions of the y-subunit in spinach chloroplasts, is conserved in Synechocystis 6803.

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“…

The atpB and the atpE genes encode for the/~ and subunits of the proton-translocation ATPase complex in prokaryotes, mitochondria and chloroplasts. In contrast, the cyanobacterial and green plastid atpB and atpE genes form a separate 'atpB' cluster which is encoded by the chloroplastic genome in plants [3,4].Little is known about the organization of AT-Pase genes in brown and red algae. In contrast, the cyanobacterial and green plastid atpB and atpE genes form a separate 'atpB' cluster which is encoded by the chloroplastic genome in plants [3,4].

Little is known about the organization of AT-Pase genes in brown and red algae.

…”

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confidence: 99%

Nucleotide sequences of theatpB and theatpE genes of the brown algaPylaiella littoralis (L.) Kjellm

et al. 1992

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The atpB and the atpE genes encode for the/~ and subunits of the proton-translocation ATPase complex in prokaryotes, mitochondria and chloroplasts. In E. coli and e-purple eubacteria the genes for all subunits of the ATPase complex are linked and constitute a single transcriptional unit [1,2]. In contrast, the cyanobacterial and green plastid atpB and atpE genes form a separate 'atpB' cluster which is encoded by the chloroplastic genome in plants [3,4].Little is known about the organization of AT-Pase genes in brown and red algae. In this report we present the nucleotide sequence of the atpB-atpE region encoded by the chloroplastic genome of the brown alga PylaieIla littoralis (L.) Kjellm (Fig. 1).The 4.2 kb Eco RI chloroplastic DNA fragment E13 of P. littoralis [5] hybridized with a spinach atpB probe [6] and was sequenced in both directions using the dideoxy sequencing method and synthetic oligonucleotides (Eurogentec S.A., Libge, Belgium). This region contains two adjacent open reading frames, which by comparison with other known sequences have been identified as the atpB and atpE genes. Their lengths are 1446 bp (482 codons) and 399 bp (133 codons) respectively. They are separated by a 14 nucleotide spacer region (Fig. 1).Comparisons with homologous genes from prokaryotes and green plastids (Figs. 2 and 3) indicate that the atpB genes are, in all cases, more conserved than the atpE genes. The percentages of identical amino acid residues between the atpB and atpE genes of P. littoralis and those of other species (calculated from the alignments, data not shown) indicate that these genes probably have a cyanobacterial origin as do those of green plastids [5].Because of the similar organisation of this region to that of other plants it appears probable that these genes are also cotranscribed [4]. Figure 4 shows the similarities in the organization of the junction region between the atpB and atpE genes of land plants and P. littoralis. It is noteworthy that the AAATGA sequence, which in land plants comprises the atpB stop codon and the atpE start codon (implying a slide backwards of ribosomes to the -1 frame on mRNA) is exactly conserved at the same position in P. littora-Iis, although the putative atpB stop codon is 12The nucleotide sequence data reported will appear in the EMBL, GenBank and DDBJ Nucleotide Sequence Databases underthe accession number X60329.

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The chloroplast genes encoding subunits of the H+-ATP synthase

Cited by 31 publications

References 86 publications

Quantitative immunochemical evidence for identical topography of subunits CF₀II and CF₀I within the photosynthetic ATP‐synthase of spinach chloroplasts

Quantitative immunochemical evidence for identical topography of subunits CF₀II and CF₀I within the photosynthetic ATP‐synthase of spinach chloroplasts

The primary structure of the γ‐subunit of the ATPase from Synechocystis 6803

Nucleotide sequences of theatpB and theatpE genes of the brown algaPylaiella littoralis (L.) Kjellm

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The chloroplast genes encoding subunits of the H+-ATP synthase

Cited by 31 publications

References 86 publications

Quantitative immunochemical evidence for identical topography of subunits CF0II and CF0I within the photosynthetic ATP‐synthase of spinach chloroplasts

Quantitative immunochemical evidence for identical topography of subunits CF0II and CF0I within the photosynthetic ATP‐synthase of spinach chloroplasts

The primary structure of the γ‐subunit of the ATPase from Synechocystis 6803

Nucleotide sequences of theatpB and theatpE genes of the brown algaPylaiella littoralis (L.) Kjellm

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Quantitative immunochemical evidence for identical topography of subunits CF₀II and CF₀I within the photosynthetic ATP‐synthase of spinach chloroplasts

Quantitative immunochemical evidence for identical topography of subunits CF₀II and CF₀I within the photosynthetic ATP‐synthase of spinach chloroplasts