Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP‐synthase

Fromme, Petra; Gräber, Peter; Salnikow, Johann

doi:10.1016/0014-5793(87)81011-6

Cited by 50 publications

(16 citation statements)

References 34 publications

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“…The structure of the F~-part from mitochondria was reported recently with a resolution of 2.8 A [1]. In chloroplasts the CF~-part has five different subunits with the stoichiometry ~3~3~t~/~ [2,3], the CF0-part has four subunits [4] and has presumably the stoichiometry I II 11112 IV [5].…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 95%

Electron cryomicroscopy of two‐dimensional crystals of the H⁺‐ATPase from chloroplasts

et al. 1995

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The H+-ATPase from spinach chloroplasts was isolated and purified. Two-dimensional crystals were obtained from the protein/lipid/detergent micelles by treatment with phospholipase and simultaneous removal of detergent and fatty acids by Biobeads. The resulting two-dimensionally ordered arrays were investigated by electron cryomicroscopy. The ordered arrays showed top view projections of CFoF 1. The images were analysed by correlation averaging. In this view CFoFI has dimensions of 11.4 × 9 nm. The average view shows a strongly asymmetric molecule, in contrast to the rather hexagonal features of CF1, previously analyzed from two-dimensional arrays. It is concluded that this is due either to an asymmetric structure and positioning of CFo relative to CF ! or to a rearrangement of CF 1 suhunits induced by binding of CF0 to CF1.Key words: Chloroplast; H+-ATPase; Two-dimensional crystal; Electron cryomicroscopy demonstrated for reconstituted CFoF~ [11]. The thin layer of ice gives the molecules a relatively large number of possibilities to be oriented. Image processing of the different orientations is difficult due to the low signal-to-noise ratio, finding the proper orientation and combining only particles which have the same orientation even more. The difficulties increase with decreasing molecular mass but can be circumvented substantially if proteins can be ordered in two-dimensional crystals or two-dimensional arrays. The arrays restrict the number of possible orientations, which facilitates the analysis considerably. The size and packing quality of the crystals determine the resolution that can be obtained. For large arrays (over 5/~m diameter) of small proteins atomic resolution has been obtained in two cases [12,13]. Recently, the analysis of negatively stained two-dimensional crystals of mitochondrial H+-ATPase has been reported [14]. In this work, we have investigated two-dimensional crystals of CFoF~ by electron cryomicroscopy using image analysis for improvement of the signal to noise ratio.

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Section: Introduction 2 Materials and Methodsmentioning

confidence: 95%

Electron cryomicroscopy of two‐dimensional crystals of the H⁺‐ATPase from chloroplasts

et al. 1995

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“…The obtained N-terminal amino acid sequence resembles the amino acid sequence of subunit IV of CF0 from spinach chloroplasts. The gene product of spinach atpI lacks the first 18 amino acids, suggesting posttranslational processing [19]. Since the start of the Chlamydomonas protein corresponds with the beginning of the mature spinach protein, it is possible that the Chlamydomonas protein is a processed product as well.…”

Section: Atpase Activitymentioning

confidence: 99%

Isolation of CF₀CF₁ from Chlamydomonas reinhardtii cw15 and the N‐terminal amino acid sequences of the CF₀CF₁ subunits

et al. 1995

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“…This is mainly the result of a deletion at the aminoterminus. In spinach, a small leader peptide is posttranslationally removed from the aminoterminus of subunit IV [13].…”

Section: Features Of the Atp Genesmentioning

confidence: 99%

Organization of plastid-encoded ATPase genes and flanking regions including homologues of infB and tsf in the thermophilic red alga Galdieria sulphuraria

Kostrzewa

Zetsche

1993

Plant Mol Biol

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We have cloned and sequenced the plastid ATPase operons (atp1 and atp2) and flanking regions from the unicellular red alga Galdieria sulphuraria (Cyanidium caldarium). Six genes (5 atpI, H, G, F, D and A 3) are linked in atp1 encoding ATPase subunits a, c, b, b, delta and alpha, respectively. The atpF gene does not contain an intron and overlaps atpD by 1 bp. As in the genome of chloroplasts from land plants, the cluster is located downstream of rps2, but between this gene and atp1 we found the gene for the prokaryotic translation elongation factor TS. Downstream of atpA, we detected two open reading frames, one encoding a putative transport protein. The genes atpB and atpE, encoding ATPase subunits beta and epsilon, respectively, are linked in atp2, separated by a 2 bp spacer. Upstream of atpB, an uninterrupted orf167 was detected which is homologous to an intron-containing open reading frame in land plant chloroplasts. This orf167 is preceded on the opposite DNA strand by a homologue to initiation factor 2 in prokaryotes. The arrangement of atp1 and atp2 is the same as observed in the multicellular red alga Antithamnion sp., indicating a conserved genome arrangement in the red algal plastid genome. Differences compared to green chloroplast genomes suggest a large phylogenetic distance between red algae and green plants, while similarities in arrangement and sequence to chromophytic ATPase operons support a red algal origin of chlorophyll a/c-containing plastids or alternatively point to a common prokaryotic endosymbiont.

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Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP‐synthase

Cited by 50 publications

References 34 publications

Electron cryomicroscopy of two‐dimensional crystals of the H⁺‐ATPase from chloroplasts

Electron cryomicroscopy of two‐dimensional crystals of the H⁺‐ATPase from chloroplasts

Isolation of CF₀CF₁ from Chlamydomonas reinhardtii cw15 and the N‐terminal amino acid sequences of the CF₀CF₁ subunits

Organization of plastid-encoded ATPase genes and flanking regions including homologues of infB and tsf in the thermophilic red alga Galdieria sulphuraria

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Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP‐synthase

Cited by 50 publications

References 34 publications

Electron cryomicroscopy of two‐dimensional crystals of the H+‐ATPase from chloroplasts

Electron cryomicroscopy of two‐dimensional crystals of the H+‐ATPase from chloroplasts

Isolation of CF0CF1 from Chlamydomonas reinhardtii cw15 and the N‐terminal amino acid sequences of the CF0CF1 subunits

Organization of plastid-encoded ATPase genes and flanking regions including homologues of infB and tsf in the thermophilic red alga Galdieria sulphuraria

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Electron cryomicroscopy of two‐dimensional crystals of the H⁺‐ATPase from chloroplasts

Electron cryomicroscopy of two‐dimensional crystals of the H⁺‐ATPase from chloroplasts

Isolation of CF₀CF₁ from Chlamydomonas reinhardtii cw15 and the N‐terminal amino acid sequences of the CF₀CF₁ subunits