F<sub>1</sub>‐Like ATPase from Anaerobic Bacterium <i>Lactobacillus casei</i> Contains Six Similar Subunits

Biketov, S F; Kasho, Vladimir N.; Kozlov, I. A.; Mileykovskaya, Yevgenia I.; Ostrovsky, D. N.; Skulachev, Vladimir P.; Tikhonova, G. V.; Tsuprun, Vladimir

doi:10.1111/j.1432-1033.1982.tb07045.x

Cited by 24 publications

(12 citation statements)

References 58 publications

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“…The active part of the enzyme appears to be composed of one subunit, which is a situation observed in Lactobacillus casei (Biketov et al 1982;Tikhonova et al 1983). Other subunits might be lost during isolation and purification, but reconstitution with activity onto depleted membranes tends to negate this possibility, as does the isolation of all subunits Can.…”

Section: Discussionmentioning

confidence: 92%

The ultrastructure and ATPase nature of polar membrane in Campylobacter jejuni

Brock¹,

Murray²

1988

Can. J. Microbiol.

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Polar membrane in Campylobacter jejuni has been visualized on membrane vesicles. It was composed of doughnut-shaped particles 5-6 nm in diameter, with stalks, arranged in a hexagonal array. This structure was stabilized on the membrane by a high ionic strength buffer in the presence of 2-mercaptoethanol. Histochemical staining indicated localized ATPase activity at the poles of the cells. An ATPase with distinctive properties has been isolated and purified from this organism; it gives a specific activity of approximately 0.3 units/mg of protein. Electron microscopy showed doughnut-shaped particles 5-6 nm in diameter. Nondissociating and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed, respectively, a single band with ATPase activity and a molecular weight of ca. 75,000 Da. The enzyme was cold labile and activity was abolished by trypsin. Dicyclohexylcarbodiimide inhibited the membrane-bound form of the enzyme, but did not inhibit the soluble form. Oligomycin had no inhibitory activity on either form of the enzyme. The enzyme specifically hydrolysed ATP, but other nucleotide substrates were not degraded. The enzyme was activated by Mg2+ and inhibited by Ca2+, whereas other ions had no effect on activity. Antibodies prepared to this enzyme bound to the polar regions of whole cells as shown by protein A - colloidal gold immunoelectron microscopy. The antibodies to this ATPase cross reacted (shown by Western blotting) with four proteins from a whole-cell extract of this organism, two proteins in Aquaspirillum serpens MW5, and three proteins from Escherichia coli K12. They did not cross-react with any proteins from Spirillum volutans, Methanococcus voltae, Vibrio cholerae, or rat liver mitochondria. Antibodies raised against the F1-ATPase of E. coli K12 cross reacted with six proteins in a whole-cell extract of this organism, and one protein species in each of the whole-cell extracts of V. cholera, A. serpens MW5, S. volutans, and rat liver mitochondria. These antibodies did not recognize any whole cell proteins from either C. jejuni or M. voltae. These results along with the ATPase activity localized by histochemical staining suggest that polar membrane is an assembly of ATPase molecules at the poles of the cell and that the ATPase isolated from C. jejuni is serologically and structurally unusual.

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Section: Discussionmentioning

confidence: 92%

The ultrastructure and ATPase nature of polar membrane in Campylobacter jejuni

Brock¹,

Murray²

1988

Can. J. Microbiol.

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“…luteus. The target sizes of these enzymes (176 f 5 kDa and 275 33 kDa respectively) proved to resemble their molecular masses [3,121. The use of doses determined by means of a dosimeter operating at +20°C is the probable reason for an approximately 1.3-times underestimate of molecular masses.…”

Section: Resultsmentioning

confidence: 99%

“…Earlier we put forward a suggestion that it is the hydrolytic function of the L. casei ATPase that determines its simple structure [3]. Thus, the evolution of the enzyme structure to involve the a-type subunits might be considered in connection with the development of the ATP synthase function.…”

Section: Resultsmentioning

confidence: 99%

“…ATPase (EC 3.6.1.34); pyruvate kinase (EC 2.7.1.40); lactate dehydrogenase (EC 1.1.1.27). described previously [3]. The soluble ATPase of L. casei was isolated from the membranes by EDTA extraction according to [3] and then purified by gel filtration through a column packed with Toyopearl HW-55F gel (Toyo Soda, Japan) in 10 mM Tris/HCl buffer containing 100 mM KC1 (pH 7.8).…”

Section: Methodsmentioning

confidence: 99%

“…We have previously shown that the membranes of the anaerobic bacterium Lactobacillus casei, which lack a respiratory chain, carry a N,N-dicyclohexylcarbodiimide-sensitive H+-ATPase [3].…”

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confidence: 99%

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Some pecularities of functioning of H⁺‐ATPase from the membranes of the anaerobic bacterium Lactobacillus casei

Mileykovskaya

Abuladze

Kormer

et al. 1987

European Journal of Biochemistry

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Radiation inactivation analysis gave the target sizes of 176 & 5 kDa and 275 33 kDa for ATPase from anaerobic Lactobacillus casei and aerobic Micrococcus luteus bacteria respectively. The values are close to the known molecular masses of the enzymes. Thus, to function the L. casei ATPase, like the F1-ATPases, requires a complete structure composed of all the enzyme subunits. L. casei ATPase is inhibited by 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole owing to modification of an amino acid residue(s) with pK > 8.5. L. casei ATPase consists of six identical subunits and differs from ct3P3y&-type F1-ATPases in a number of catalytic properties. Namely, ATP hydrolysis under the 'unisite' conditions proceeds at a relatively high rate suggesting the absence of cooperative interactions between the catalytic sites. Contrary to mitochondria1 F1-ATPase. L. casei ATPase does not form an inactive complex with ADP. These findings imply essential differences in the operating mechanism for L. casei ATPase and F1 ATPase.Unravelling the molecular mechanism of the H ' -ATPase

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Electron microscopy of the F₁F₀ ATP synthase: From structure to function

Gogol¹

1994

Microscopy Res & Technique

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The F1F0 ATP synthase is the large multisubunit complex which uses the proton gradient of energetically active membranes to synthesize ATP. While biochemical and genetic approaches have characterized the composition of the enzyme and elucidated many details of its mechanism and assembly, electron microscopy has been the tool of primary importance in determining the arrangement of the many subunits which comprise the F1F0. The highly cooperative catalytic mechanism is tightly coupled to transmembrane proton translocation in a separate and rather distant sector of the complex. An understanding of this intricate process and its control requires an appreciation of subunit interactions, starting with their locations relative to one another. Electron microscopy has provided most of the available structural information on the F1F0, and recent applications of cryo-electron microscopy have captured different functionally relevant configurations which may finally address longstanding questions about subunit rearrangements during the catalytic cycle.

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F₁‐Like ATPase from Anaerobic Bacterium Lactobacillus casei Contains Six Similar Subunits

Cited by 24 publications

References 58 publications

The ultrastructure and ATPase nature of polar membrane in Campylobacter jejuni

The ultrastructure and ATPase nature of polar membrane in Campylobacter jejuni

Some pecularities of functioning of H⁺‐ATPase from the membranes of the anaerobic bacterium Lactobacillus casei

Electron microscopy of the F₁F₀ ATP synthase: From structure to function

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F1‐Like ATPase from Anaerobic Bacterium Lactobacillus casei Contains Six Similar Subunits

Cited by 24 publications

References 58 publications

The ultrastructure and ATPase nature of polar membrane in Campylobacter jejuni

The ultrastructure and ATPase nature of polar membrane in Campylobacter jejuni

Some pecularities of functioning of H+‐ATPase from the membranes of the anaerobic bacterium Lactobacillus casei

Electron microscopy of the F1F0 ATP synthase: From structure to function

Contact Info

Product

Resources

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F₁‐Like ATPase from Anaerobic Bacterium Lactobacillus casei Contains Six Similar Subunits

Some pecularities of functioning of H⁺‐ATPase from the membranes of the anaerobic bacterium Lactobacillus casei

Electron microscopy of the F₁F₀ ATP synthase: From structure to function