Interaction between the oligomycin sensitivity conferring protein and the F0 sector of the mitochondrial adenosinetriphosphatase complex : cooperative effect of the F1 sector
Beef heart mitchondrial oligomycin sensitivity conferring protein (OSCP) labeled with [14C]-N-ethylmaleimide ([14C]OSCP) at the only cysteine residue, Cys-118, present in the sequence [Ovchinnikov, Y. A., Modyanov, N. N., Grinkevich, V. A., Aldanova, N. A., Trubetskaya, O. E., Nazimov, I.V., Hundal, T., & Ernster, L. (1984) FEBS Lett. 166, 19-22] exhibits full biological activity in a reconstituted F0-F1 system [Dupuis, A., Issartel, J. P., Lunardi, J., Satre, M., & Vignais, P. V. (1985) Biochemistry 24, 728-733]. The binding parameters of [14C]OSCP with respect to the F0 sector of submitochondrial particles largely depleted of F1 and OSCP (AUA particles) have been explored. In the absence of added F1, a limited number of high-affinity OSCP binding sites were detected in the AUA particles (20-40 pmol/mg of particles); under these conditions, the low-affinity binding sites for OSCP were essentially not saturable. Addition of F1 to the particles promoted high-affinity binding for OSCP, with an apparent Kd of 5 nM, a value 16 times lower than the Kd relative to the binding of OSCP to F1 in the absence of particles. Saturation of the F1 and OSCP binding sites of AUA particles was attained with about 200 pmol of both F1 and OSCP added per milligram of particles. The oligomycin-dependent inhibition of F1-ATPase bound to AUA particles was assayed as a function of bound OSCP. At subsaturating concentrations of F1, the dose-effect curves were rectilinear until inhibition of ATPase activity by oligomycin was virtually complete, and maximal inhibition was obtained for an OSCP to F1 ratio of 1 (mol/mol).(ABSTRACT TRUNCATED AT 250 WORDS).
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
1987 |
|---|---|
| Erschienen: |
1987 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:26 |
|---|---|
| Enthalten in: |
Biochemistry - 26(1987), 2 vom: 27. Jan., Seite 410-8 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Dupuis, A [VerfasserIn] |
|---|
| Anmerkungen: |
Date Completed 20.05.1987 Date Revised 10.12.2019 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM028629035 |
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| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM028629035 | ||
| 003 | DE-627 | ||
| 005 | 20231221110231.0 | ||
| 007 | tu | ||
| 008 | 231221s1987 xx ||||| 00| ||eng c | ||
| 028 | 5 | 2 | |a pubmed24n0096.xml |
| 035 | |a (DE-627)NLM028629035 | ||
| 035 | |a (NLM)2881578 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Dupuis, A |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Interaction between the oligomycin sensitivity conferring protein and the F0 sector of the mitochondrial adenosinetriphosphatase complex |b cooperative effect of the F1 sector |
| 264 | 1 | |c 1987 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 500 | |a Date Completed 20.05.1987 | ||
| 500 | |a Date Revised 10.12.2019 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Beef heart mitchondrial oligomycin sensitivity conferring protein (OSCP) labeled with [14C]-N-ethylmaleimide ([14C]OSCP) at the only cysteine residue, Cys-118, present in the sequence [Ovchinnikov, Y. A., Modyanov, N. N., Grinkevich, V. A., Aldanova, N. A., Trubetskaya, O. E., Nazimov, I.V., Hundal, T., & Ernster, L. (1984) FEBS Lett. 166, 19-22] exhibits full biological activity in a reconstituted F0-F1 system [Dupuis, A., Issartel, J. P., Lunardi, J., Satre, M., & Vignais, P. V. (1985) Biochemistry 24, 728-733]. The binding parameters of [14C]OSCP with respect to the F0 sector of submitochondrial particles largely depleted of F1 and OSCP (AUA particles) have been explored. In the absence of added F1, a limited number of high-affinity OSCP binding sites were detected in the AUA particles (20-40 pmol/mg of particles); under these conditions, the low-affinity binding sites for OSCP were essentially not saturable. Addition of F1 to the particles promoted high-affinity binding for OSCP, with an apparent Kd of 5 nM, a value 16 times lower than the Kd relative to the binding of OSCP to F1 in the absence of particles. Saturation of the F1 and OSCP binding sites of AUA particles was attained with about 200 pmol of both F1 and OSCP added per milligram of particles. The oligomycin-dependent inhibition of F1-ATPase bound to AUA particles was assayed as a function of bound OSCP. At subsaturating concentrations of F1, the dose-effect curves were rectilinear until inhibition of ATPase activity by oligomycin was virtually complete, and maximal inhibition was obtained for an OSCP to F1 ratio of 1 (mol/mol).(ABSTRACT TRUNCATED AT 250 WORDS) | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Carrier Proteins |2 NLM | |
| 650 | 7 | |a Macromolecular Substances |2 NLM | |
| 650 | 7 | |a Membrane Proteins |2 NLM | |
| 650 | 7 | |a Oligomycins |2 NLM | |
| 650 | 7 | |a Tritium |2 NLM | |
| 650 | 7 | |a 10028-17-8 |2 NLM | |
| 650 | 7 | |a Dicyclohexylcarbodiimide |2 NLM | |
| 650 | 7 | |a 538-75-0 |2 NLM | |
| 650 | 7 | |a Adenosine Triphosphatases |2 NLM | |
| 650 | 7 | |a EC 3.6.1.- |2 NLM | |
| 650 | 7 | |a Mitochondrial Proton-Translocating ATPases |2 NLM | |
| 650 | 7 | |a EC 3.6.3.- |2 NLM | |
| 650 | 7 | |a Proton-Translocating ATPases |2 NLM | |
| 650 | 7 | |a EC 3.6.3.14 |2 NLM | |
| 650 | 7 | |a oligomycin sensitivity-conferring protein |2 NLM | |
| 650 | 7 | |a EC 7.1.2.2 |2 NLM | |
| 650 | 7 | |a Ethylmaleimide |2 NLM | |
| 650 | 7 | |a O3C74ACM9V |2 NLM | |
| 700 | 1 | |a Vignais, P V |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Biochemistry |d 1962 |g 26(1987), 2 vom: 27. Jan., Seite 410-8 |w (DE-627)NLM000000469 |x 1520-4995 |7 nnns |
| 773 | 1 | 8 | |g volume:26 |g year:1987 |g number:2 |g day:27 |g month:01 |g pages:410-8 |
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| 952 | |d 26 |j 1987 |e 2 |b 27 |c 01 |h 410-8 | ||