Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondria

Ovchinnikov, Yu.A.; Modyanov, Nikolaï N.; Grinkevich, V.A.; Aldanova, N.A.; Kostetsky, P. V.; Trubetskaya, O. E.; Hundal, Torill; Ernster, Lars

doi:10.1016/0014-5793(84)80580-3

Cited by 22 publications

(5 citation statements)

References 25 publications

(9 reference statements)

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“…The 8 and « subunits of TFi are similar in sequence to the corresponding subunits in E. coli Fi (Ohta et al, 1988). The e subunit of E. coli Fi is structurally equivalent to the 8 subunit of MFi (Walker et al, 1982), whereas the 8 subunit of E. coli Ft is equivalent to the oligomycin sensitivity conferring protein (OSCP), which is a component of mitochondrial F0 (Ovchinnikov et al, 1984). The « subunit of MFi is unique to mitochondrial Fi-ATPases (Walker et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

Inhibition and inactivation of the F1 adenosine triphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide

Paik

Jault²,

Allison³

1994

Biochemistry

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The F1-ATPase from Bacillus PS3 (TF1) hydrolyzes 50 microM ATP in three kinetic phases. An initial burst rapidly decelerates to a partially inhibited, intermediate phase, which, in turn, gradually accelerates to an uninhibited, final steady-state rate. Lauryl dimethylamine oxide (LDAO) stimulates the final rate over 4-fold. The stimulatory effect saturates at about 0.1% LDAO. Under these conditions, the intermediate phase is nearly absent. Dequalinium inhibits TF1 reversibly in the dark in the presence or absence of LDAO. The apparent affinity of TF1 for dequalinium increases in the presence of LDAO. Dixon plots of the initial rates of the intermediate phase and the final rates against dequalinium concentration at a series of fixed ATP concentrations in the presence and absence of 0.03% LDAO indicate noncompetitive inhibition in each case. Replots of the slopes of the Dixon plots for the initial rate of the intermediate phase and the final rate against 1/[ATP] reveal apparent Km values of 770 microM and 144 microM, respectively, when obtained in the absence of LDAO. The apparent Km values determined from the data obtained in the presence of LDAO for the same phases are 303 microM and 163 microM, respectively. These results suggest that LDAO stimulates ATPase activity either by increasing the affinity of noncatalytic sites for ATP, which promotes release of inhibitory MgADP from a catalytic site, or by directly promoting release of MgADP from the affected catalytic site. Dequalinium retards this process without affecting the affinity of noncatalytic sites for ATP. When irradiated in the presence of dequalinium, TF1 is rapidly inactivated with an apparent Kd of 12.5 microM in the presence or absence of LDAO.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 99%

Inhibition and inactivation of the F1 adenosine triphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide

Paik

Jault²,

Allison³

1994

Biochemistry

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“…(In the following, we will consider these proteins as Fo components.) Both proteins have been isolated from intact mitochondria and the amino acid sequences have been determined recently (43,142). OSCP is a basic protein of Mr 20,967 and exhibits regions of homology to the sequence of the E. coli 8 subunit in F1 (142,216,218); the latter has been demonstrated to be essential for the binding of F1 to Fo (195).…”

Section: Subunit Compositionmentioning

confidence: 99%

Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.

Schneider¹,

Altendorf²

1987

Microbiological Reviews

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“…This difference in stoichiometry means that either another subunit fulfills the role of the second copy of subunit b or the stator stalk has a different composition in the mitochondrial enzyme of eukaryotes. It should be noted that considerable (ϳ30%) homology has been reported between bovine OSCP and the hydrophilic region of E. coli subunit b (25). Thus, OSCP in the eukaryotic complex may fulfill the role of both the second subunit b and subunit ␦.…”

Section: Discussionmentioning

confidence: 99%

Single Copies of Subunits d, Oligomycin-sensitivity Conferring Protein, and b Are Present in the Saccharomyces cerevisiaeMitochondrial ATP Synthase

Bateson

Devenish

Nagley

et al. 1999

Journal of Biological Chemistry

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In the mitochondrial ATP synthase (mtATPase) of the yeast Saccharomyces cerevisiae, the stoichiometry of subunits d, oligomycin-sensitivity conferring protein (OSCP), and b is poorly defined. We have investigated the stoichiometry of these subunits by the application of hexahistidine affinity purification technology. We have previously demonstrated that intact mtATPase complexes incorporating a Hex 6 -tagged subunit can be isolated via Ni 2؉ -nitrilotriacetic acid affinity chromatography (Bateson, M., Devenish, R. J., Nagley, P., and Prescott, M. (1996) Anal. Biochem. 238, 14 -18). Strains were constructed in which Hex 6 -tagged versions of subunits d, OSCP, and b were coexpressed with the corresponding wild-type subunit. This coexpression resulted in a mixed population of mtATPase complexes containing untagged wild-type and Hex 6 -tagged subunits. The stoichiometry of each subunit was then assessed by determining whether or not the untagged wild-type subunit could be recovered from Ni 2؉ -nitrilotriacetic acid purifications as an integral component of those complexes absorbed by virtue of the Hex 6 -tagged subunit. As only the Hex 6 -tagged subunit was recovered from such purifications, we demonstrate that the stoichiometry of subunits d, OSCP, and b in yeast is 1 in each case.

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Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondria

Cited by 22 publications

References 25 publications

Inhibition and inactivation of the F1 adenosine triphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide

Inhibition and inactivation of the F1 adenosine triphosphatase from Bacillus PS3 by dequalinium and activation of the enzyme by lauryl dimethylamine oxide

Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.

Single Copies of Subunits d, Oligomycin-sensitivity Conferring Protein, and b Are Present in the Saccharomyces cerevisiaeMitochondrial ATP Synthase

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