Effect of calcium on the interactions between Ca2+-ATPase molecules in sarcoplasmic reticulum

Keresztes, T.; Jóna, István; Pikula, Sławomir; Végh, Marcell Zoltán; Müllner, Nándor; Papp, S.; Martonosi, Anthony

doi:10.1016/0005-2736(89)90300-3

Cited by 14 publications

(6 citation statements)

References 66 publications

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“…In analogy to various biochemical findings [14][15][16][17] and electron microscopical data which suggest an oligomeric structure for the SR Ca2+-ATPase [13], we provide in this report biochemical evidence that this abundant muscle calcium ion pump exists in its native membrane environment as a quaternary structure in a multi-copy complex of 110 kDa units. Previous crosslinking studies of the sarcoplasmic reticulum used protein gels for the analysis of the microsomal 110 kDa protein [18][19][20][21][22].…”

Section: Resultssupporting

confidence: 82%

“…In addition, exclusion chromatography of detergent solubilized Ca2+-ATPase preparations [14], fluorescence energy transfer measurements of native and reconstituted membranes [15], kinetic measurements on calcium translocation [16] and radiation inactivation studies of the Ca2+-ATPase [17] all argue in favor of oligomeric SERCA structures. In addition, previous crosslinking studies of SR membranes indicate that a 110 kDa protein exhibits a tendency to form oligomeric forms as reviewed by Andersen [18].…”

Section: Introductionmentioning

confidence: 99%

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Oligomerization of sarcoplasmic reticulum Ca²⁺‐ATPase from rabbit skeletal muscle

Maguire

Ohlendieck

1996

FEBS Letters

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Although the primary structure and catalytic cycle of the sarcoplasmic reticulum Ca2+-ATPasc has been revealed, it is not well understood whether functional Ca 2+ pump proteins exist in a monomeric or an oligomeric state in native skeletal muscle membranes. Here, we show that the Ca2+-ATPase tends to form high molecular weight complexes, estimated to be dimers and tetramers using immunoblotting of two-dimensionally separated microsomal membranes following crosslinking. This agrees with both electron microscopical and biochemical findings which demonstrate that Ca2+-ATPase clusters are the predominant molecular species in native membranes and that oligomerization may play a role in cooperative kinetics and enzyme stabilization.

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Section: Resultssupporting

confidence: 82%

Section: Introductionmentioning

confidence: 99%

Oligomerization of sarcoplasmic reticulum Ca²⁺‐ATPase from rabbit skeletal muscle

Maguire

Ohlendieck

1996

FEBS Letters

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“…Considering the relative molecular sizes of fluorescein and the ATPasemonomer, and the small Ro value of the Co2+/ fluorescein donor/acceptor pair, more than two neighbouring and equidistant sites seems an unrealistic possibility. This distance estimation is consistent with the experimental observations published by Mata and Gutierrez-Merino [22] and by Highsmith and Cohen [43], and more recently by Keresztes et al [44] showing a partial depolarization of fluorescein in labeled sarcoplasmic reticulum membranes.…”

Section: Ffuorirnetric Studiessupporting

confidence: 92%

Distances between functional sites of the Ca²⁺+ Mg²⁺‐ATPase from sarcoplasmic reticulum using Co²⁺ as a spectroscopic ruler

Cuenda¹,

Henao²,

Gutiérrez‐Merino³

1990

European Journal of Biochemistry

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Cobalt ion inhibits the Ca2+ + Mg2 +-ATPase activity of sealed sarcoplasmic reticulum vesicles, of solubilized membranes and of the purified enzyme. To use Co2+ appropriately as a spectroscopic ruler to map functional sites of the Ca2+ + Mg2+-ATPase, we have carried out studies to obtain the kinetic parameters needed to define the experimental conditions to conduct the fluorimetric studies.1. The apparent Ko.5 values of inhibition of this ATPase are 1.4 mM, 4.8 mM and 9.5 mM total Co2+ at pH 8.0, 7.0 and 6.0, respectively. The inhibition by Co2+ is likely to be due to free Co2+ binding to the enzyme. Millimolar Ca2 from which we obtain a distance of 1.1 -1.9 nm between Co2+ and fluorescein located at neighbouring catalytic sites. Co2+. ATP can be used as a substrate by this enzyme with V,,, of 2.4 f 0.2 pmol ATP hydrolyzed min- Co2+ partially quenches, about 10The sarcoplasmic reticulum Ca2+ + Mg2 +-ATPase uses Mg2+ . ATP as its physiological substrate and couples ATP hydrolysis to the active transport of Ca" across this membrane [l]. Binding of two Ca2+ ions to high-affinity binding sites/ATPase molecule is step that precedes Ca2+ transport to the luminal space of sarcoplasmic reticulum [l, 21. To understand better the Ca2+ transport process coupled to ATP hydrolysis requires complementary experimental information obtained by using kinetic and structural studies of this enzyme. In this regard, the location of Ca2+ and ATP binding sites relative to each other is an important issue; there is a large range of values for the distance between these sites on ATPase reported by different groups of investigators, i. e. 1 -6 nm [3 -71. Forster energy transfer between different donor/acceptor pairs of fluorescent targets selectively bound to these sites has been used to obtain these estimations. On the other hand, Xray diffraction studies [8, 91 and image processing of electron microscopy data [lo, 111 have provided evidence for an overall shape of an ATPase unit protruding about 4.0 -6.0 nm from the lipid/water interface and having a cross-sectional diameter of the cytosolic lobule of approximately 8.0-9.0 nm in its dimeric form, which is probably the predominant state in

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“…2). This may be due to inactivation of the active Ca-+ transporting enzyme in the presence of high levels of detergent which causes dissociation of oligomeric proteins (14,17,25) and the removal of phospholipids required for the activity (15,19).…”

Section: Discussionmentioning

confidence: 99%

Solubilization and Reconstitution of Ca²⁺ Pump from Corn Leaf Plasma Membrane

Kasai

Muto²

1991

Plant Physiol.

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Effect of calcium on the interactions between Ca2+-ATPase molecules in sarcoplasmic reticulum

Cited by 14 publications

References 66 publications

Oligomerization of sarcoplasmic reticulum Ca²⁺‐ATPase from rabbit skeletal muscle

Oligomerization of sarcoplasmic reticulum Ca²⁺‐ATPase from rabbit skeletal muscle

Distances between functional sites of the Ca²⁺+ Mg²⁺‐ATPase from sarcoplasmic reticulum using Co²⁺ as a spectroscopic ruler

Solubilization and Reconstitution of Ca²⁺ Pump from Corn Leaf Plasma Membrane

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Effect of calcium on the interactions between Ca2+-ATPase molecules in sarcoplasmic reticulum

Cited by 14 publications

References 66 publications

Oligomerization of sarcoplasmic reticulum Ca2+‐ATPase from rabbit skeletal muscle

Oligomerization of sarcoplasmic reticulum Ca2+‐ATPase from rabbit skeletal muscle

Distances between functional sites of the Ca2++ Mg2+‐ATPase from sarcoplasmic reticulum using Co2+ as a spectroscopic ruler

Solubilization and Reconstitution of Ca2+ Pump from Corn Leaf Plasma Membrane

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Oligomerization of sarcoplasmic reticulum Ca²⁺‐ATPase from rabbit skeletal muscle

Oligomerization of sarcoplasmic reticulum Ca²⁺‐ATPase from rabbit skeletal muscle

Distances between functional sites of the Ca²⁺+ Mg²⁺‐ATPase from sarcoplasmic reticulum using Co²⁺ as a spectroscopic ruler

Solubilization and Reconstitution of Ca²⁺ Pump from Corn Leaf Plasma Membrane