Reconstitution of Oxidative Phosphorylation in Pea Cotyledon Submitochondrial Particles

Horak, Arnost; Horak, Helena; Packer, Mary

doi:10.1007/978-1-4899-3517-5_25

Cited by 2 publications

(4 citation statements)

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“…The evidence presented here, together with that published elsewhere (Horak et al, 1987(Horak et al, , 1989Kimura et al, 1989), clearly shows that the subunit identified on the basis of its electrophoretic mobility as the 6 (26. chondria. The experiments with submitochondrial particles (Fig.…”

Section: Methodsmentioning

confidence: 65%

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Plant mitochondrial F1-ATPase. The presence of oligomycin-sensitivity-conferring protein (OSCP)

Horak

Dunbar

et al. 1989

Biochemical Journal

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Purified pea (Pisum sativum) cotyledon Fl-ATPase contains six subunits rather than the five usually reported for F1-ATPases. The additional 26.5 kDa (a) subunit is shown by immunoblotting and N-terminal amino acid sequencing to be similar to bovine oligomycin-sensitivity-conferring protein (OSCP). It is concluded that the a subunit of plant mitochondrial Fl-ATPase is the plant OSCP. This OSCP subunit occurs in all mono-and di-cotyledonous species of plants tested (maize, oats, peas, potatoes, sweet potatoes and turnips).

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Section: Methodsmentioning

confidence: 65%

“…Norling et al (1988) demonstrated a requirement for an OSCP-like protein to confer oligomycin sensitivity to potato (Solanum tuberosum) F1-ATPase in cross-reconstitution experiments with bovine heart mitochondrial membranes. Horak et al (1989) …”

Section: Introductionmentioning

confidence: 99%

Plant mitochondrial F1-ATPase. The presence of oligomycin-sensitivity-conferring protein (OSCP)

Horak

Dunbar

et al. 1989

Biochemical Journal

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“…The enzyme was purified 19-fold from submitochondrial particles with a final specific activity of 23 units/mg. This paper was followed by the identification of several of the F]-ATPase subunits (Horak et al, 1987(Horak et al, , 1989a(Horak et al, , 1990 and by functionality studies performed through membrane reconstitution and stability experiments (Horak et al, 1987(Horak et al, , 1988(Horak et al, , 1989b. The pea mitochondrial F,-ATPase has six subunits, a characteristic seen in several other preparations from plants (sweet potato root [Iwasaki andAsahi, 1983, 1985] and turnip [O'Rourke, 1988]).…”

Section: Discussionmentioning

confidence: 99%

“…101, 1993 al., 19851, and spinach leaf [Hamasur and Glaser, 19901). Horak et al (1989aHorak et al ( , 1989b showed that the sixth subunit (termed the 6-subunit by Horak and Packer, 1985) is the oligomycin sensitivity-confemng protein. This subunit is frequently lost from the enzyme preparation when harsh methods are used to liberate the F1 portion from the membrane (Horak et al, 1989b).…”

Section: Discussionmentioning

confidence: 99%

Monoclonal Antibodies to the [alpha]- and [beta]-Subunits of the Plant Mitochondrial F1-ATPase

1993

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We have generated nine monoclonal antibodies against subunits of the maize (Zea mays 1.) mitochondrial F1-ATPase. These monoclonal antibodies were generated by immunizing mice against maize mitochondrial fractions and randomly collecting useful hybridomas. To prove that these monoclonal antibodies were directed against ATPase subunits, we tested their cross-reactivity with purified F,-ATPase from pea cotyledon mitochondria. One of the antibodies (a-ATPaseD) cross-reacted with the pea F,-ATPase asubunit and two (8-ATPaseD and 8-ATPaseE) cross-reacted with the pea Fl-ATPase j3-subunit. This established that, of the nine antibodies, four react with the maize a-ATPase subunit and the other five react with the maize 8-ATPase subunit. Most of the monoclonal antibodies cross-react with the F1-ATPase from a wide range of plant species. Each of the four monoclonal antibodies raised against the a-subunit recognizes a different epitope. Of the five 8-subunit antibodies, at least three different epitopes are recognized. Direct incubation of the monoclonal antibodies with the F1-ATPase failed to inhibit the ATPase activity. lhe monoclonal antibodies a-ATPaseD and 8-ATPaseD were bound to epoxideglass QuantAffinity beads and incubated with a purified preparation of pea Fl-ATPase. lhe ATPase activity was not inhibited when the antibodies bound the ATPase. lhe antibodies were used to help map the pea F1-ATPase subunits on a two-dimensional map of whole pea cotyledon mitochondrial protein. In addition, the antibodies have revealed antigenic similarities between various isoforms observed for the a-and 8-subunits of the purified F1-ATPase. The specificity of these monoclonal antibodies, along with their cross-species recognition and their ability to bind the F1-ATPase without inhibiting enzymic function, makes these antibodies useful and invaluable tools for the further purification and characterization of plant mitochondrial F,-ATPases.Electrogenic H+-ATPases have been found in nearly a11 physiological membrane systems investigated. Each of these membrane-bound ATPases can be placed into one of severa1 groups. The three most common types of proton ATPases are E1-E2 type, Fo-F1 type, and the microsomal type (AlAwqati, 1986). The E1-E2 type ATPases are found in yeast and funga1 plasma membranes and the gastric plasma and microsomal membranes. ATPases of the microsomal type are located in the membranes of Golgi apparatus, ER, endosomes,

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Reconstitution of Oxidative Phosphorylation in Pea Cotyledon Submitochondrial Particles

Cited by 2 publications

References 4 publications

Plant mitochondrial F1-ATPase. The presence of oligomycin-sensitivity-conferring protein (OSCP)

Plant mitochondrial F1-ATPase. The presence of oligomycin-sensitivity-conferring protein (OSCP)

Monoclonal Antibodies to the [alpha]- and [beta]-Subunits of the Plant Mitochondrial F1-ATPase

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