Sarcoplasmic reticulum adenosine triphosphatase: Labeling of an essential lysyl residue with pyridoxal-5′-phosphate

Murphy, Alexander J.

doi:10.1016/0003-9861(77)90014-5

“…This may suggest that ATPase inactivation was due to modification of amino groups that are involved in an ATP binding site. Similar results were obtained with other reagents (Murphy, 1977;Pick & Karlish, 1980;Hidalgo et al, 1982), where investigators have proposed that a lysyl residue constitutes part of the active site. However, it is not clear whether this lysyl residue constitutes part of the ATP-binding site or of the phosphorylation site.…”

Section: Discussionsupporting

confidence: 87%

Chemical modification of sarcoplasmic reticulum. Stimulation of Ca2+ release

Shoshan‐Barmatz¹

1986

Biochemical Journal

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Pretreatment of sarcoplasmic membranes with acetic or maleic anhydrides, which interact principally with amino groups, resulted in an inhibition of Ca2+ accumulation and ATPase activity. The presence of ATP, ADP or adenosine 5'-[beta, gamma-imido]triphosphate in the modification medium selectively protected against the inactivation of ATPase activity by the anhydride but did not protect against the inhibition of Ca2+ accumulation. Acetic anhydride modification in the presence of ATP appeared to increase specifically the permeability of the sarcoplasmic reticulum membrane to Ca2+ but not to sucrose, Tris, Na+ or Pi. The chemical modification stimulated a rapid release of Ca2+ from sarcoplasmic reticulum vesicles passively or actively loaded with calcium, from liposomes reconstituted with the partially purified ATPase fraction but not from those reconstituted with the purified ATPase. The inactivation of Ca2+ accumulation by acetic anhydride (in the presence of ATP) was rapid and strongly pH-dependent with an estimated pK value above 8.3 for the reactive group(s). The negatively charged reagents pyridoxal 5-phosphate and trinitrobenzene-sulphonate, which also interact with amino groups, did not stimulate Ca2+ release. Since these reagents do not penetrate the sarcoplasmic reticulum membranes, it is proposed that Ca2+ release is promoted by modification of internally located, positively charged amino group(s).

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“…Lys 492 can be cross-linked with Lys 515 (asterisk) by DIDS (Hua and Inesi, 1997), consistent with a 13 Å distance that is close to the length of the ATP molecule. Lys 492 and Lys 684 react with pyridoxal phosphate and nucleotide derivatives (Murphy, 1977;Yamamoto et al, 1988;Yamagata et al, 1993), consistent with their proximity to the phosphorylation site. Lys 492 also reacts with TNP-8N3-AMP (McIntosh et al, 1992) and even more efficiently with TNP-2N3-AMP (Inesi et al, 1992a), explaining the highly protective effect of TNP-AMP from ThioGlo1.…”

Section: Discussionmentioning

confidence: 63%

Characterization of Calcium, Nucleotide, Phosphate, and Vanadate Bound States by Derivatization of Sarcoplasmic Reticulum ATPase with ThioGlo1

Hua

¹

,

Fabris

²

,

Inesi

³

1999

Biophysical Journal

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Sarcoplasmic reticulum vesicles were incubated with the maleimide-directed probe ThioGlo1, resulting in ATPase inactivation. Reacted ThioGlo1, revealed by its enhanced fluorescence, was found to be associated with the cytosolic but not with the membrane-bound region of the ATPase. The dependence of inactivation on ThioGlo1 concentration suggests derivatization of approximately four residues per ATPase, of which Cys(364), Cys(498), and Cys(636) were identified in prominently fluorescent peptide fragments. These cysteines reside within the phosphorylation and nucleotide-binding region of the ATPase. Accordingly, protection is observed in the presence of ATP, 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate (TNP-AMP), or an fluoroisothiocyanate label of Lys(515). Furthermore, protection is observed in the presence of vanadate (or decavanadate), but not in the presence of phosphate. Labeling occurs equally well in the presence or in the absence of Ca(2+) and thapsigargin, excluding a role of the E1-to-E2 transition in the protective effect of vanadate. It is concluded that protection by vanadate is due to formation of a pentacoordinated orthovanadate complex at the phosphorylation site, corresponding to a stable transition state analog of the phosphorylation reaction, with intermediate characteristics of the EP1 and EP2 states. The lack of protection by phosphate is attributed to instability of its complex with the enzyme (EP2). These findings are discussed with respect to different structural images obtained from diffraction studies of ATPase in the presence or in the absence of Ca(2+) and/or decavanadate (Ogawa et al., 1998, Biophys. J. 75:41-52).

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“…Changes in SH group reactivity connected with different states ofthe enzyme were observed by Champeil et al (76), Yamada and Ikemoto (665), Ikemoto et al (225,230), Murphy (431,433), Yoshida and Tono: mura (678), Andersen and Meller (13), Martonosi (379), and Thorley-Lawson and Green (594). The effect of ATP on the reactivity of lysyl groups was reported by Murphy (432) and by Yamamoto and Tonomura (675,676). Although the involvement of histidine residues in ATPase activity was suggested by several investigators (382,679), ATP or p-nitrophenylphosphate did not protect against the loss of ATPase activity during ethoxyformylation of the Ca 2+_ ATPase (586).…”

Section: Influence Ofatp On Mobility and Reactivity Of Protein Side-cmentioning

confidence: 83%

Mechanism of Ca²⁺Transport by Sarcoplasmic Reticulum

Martonosi

¹

,

Beeler

²

1983

Comprehensive Physiology

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The sections in this article are: Structure of Sarcoplasmic Reticulum and Transverse Tubules Structure of Plasmalemma and T Tubules Sarcoplasmic Reticulum Junction Between T Tubules and SR Mechanism of Excitation‐Contraction Coupling Isolation of SR , T Tubules, and Surface Membrane Elements from Skeletal Muscle Separation of Membrane Fractions by Calcium Oxalate or Calcium Phosphate Loading Protein Composition of SR Structure of Ca 2+ ‐Transport ATP ase and Its Disposition in SR Membrane Fragmentation of Ca 2+ ‐ ATP ase With Proteolytic Enzymes Primary Sequence of Ca 2+ ‐Transport ATP ase From Rabbit SR Structure of Proteolipids Structure and Distribution of Calsequestrin and High‐Affinity Ca 2+ ‐Binding Protein in SR Lipid Composition of SR Distribution of Phospholipids in Membrane Bilayer Role of Phospholipids in Atpase Activity and CA 2+ Transport Boundary Lipids and the Problem of Lipid Annulus Rate of ATP Hydrolysis and Physical Properties of the Lipid Phase Mobility of Phospholipids and Ca 2+ ‐Transport ATP ase in SR Mechanism of ATP Hydrolysis and CA 2+ Transport Introduction of Reaction Sequence Ca 2+ Binding to SR Binding of Ca 2+ to Ca 2+ ‐Transport ATP ase Binding of Mg 2+ to Ca 2+ ‐ ATPase Binding of ATP to Ca 2+ ‐ ATPase Binding of Various Substrates to Ca 2+ ‐ ATPase Influence of ATP on Mobility and Reactivity of Protein Side‐Chain Groups Formation of Enzyme‐Substrate Complex Formation and Properties of Phosphoproteins Kinetics of E∼P Formation Relationship Between Enzyme Phosphorylation and Translocation of Calcium Changes in Ca 2+ Affinity of Phosphoenzyme During Ca 2+ Translocation ADP ‐Sensitive and ADP ‐insensitive Phosphoprotein Intermediates Effect of Potassium on ATPase Activity and Ca 2+ Transport Reversal of the CA 2+ Pump Ca 2+ Release Induced by ADP + P i Ca 2+ Gradient‐Dependent Phosphorylation of ATPase by P i Arsenate‐Induced Ca 2+ Release Mechanism of Ca 2+ Release Induced by ADP + P i Ca 2+ Gradient‐Independent Phosphorylation of Ca 2+ ‐ ATPase by P i Role of Ca 2+ ‐Protein Interactions in ATP Synthesis P i HOH Exchange NTP P i Exchange Physical Basis of CA 2+ Translocation Protein‐Protein Interactions in SR and Their Functional Significance Electron Microscopy Fluorescence‐Energy Transfer Electron Spin Resonance Studies ATP ase‐ ATP ase Interactions in Detergent Solutions Chemical Cross‐Linking Effects of Inhibitors on ATPase Activity Possibility of Subunit Heterogeneity Conclusion Permeability of SR Monovalent‐Cation Channels in SR Anion Channels in SR Effect of Membrane Proteins on Permeability of SR Membranes Relationship Between Membrane Potential and Calcium Fluxes Across SR Membrane Probes as Indicators of SR Membrane Potential Influence of SR Membrane Potential on Calcium Permeability Influence of Membrane Potential on Active Calcium Transport Effect of Calcium Uptake on Membrane Potential of SR A Critical Analysis of Experimental Findings on Effects of Ca 2+ Transport on Membrane Potential Effect of Calcium on Optical Response of Positive Cyanine Dyes Response of Negatively Charged Dyes to Calcium Transport by SR Vesicles Membrane Potential of SR In Vivo Effect of Ca 2+ Release on Membrane Potential of SR Transport of CA 2+ by Cardiac SR Kinetic Differences Between SR of Fast‐Twitch and Slow‐Twitch Skeletal Muscles Regulation of CA 2+ Transport by Membrane Phosphorylation Role of Protein Kinase‐Dependent Membrane Phosphorylation in Regulation of Ca 2+ Transport by Skeletal Muscle SR Physiological Significance of Phospholamban Phosphorylation Biosynthesis of SR Studies on SR Development In Vivo Assembly of SR in Cultured Skeletal and Cardiac Muscle Synthesis of Ca 2+ ‐Transport ATPase in Cell‐Free Systems and Its Insertion into the Membrane Synthesis of Calsequestrin Regulation of Synthesis of Ca 2+ ‐Transport ATPase Myogenic Regulation Neural Influence on Concentration of Ca 2+ ‐ ATPase in Muscle Cells

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Sarcoplasmic reticulum adenosine triphosphatase: Labeling of an essential lysyl residue with pyridoxal-5′-phosphate

Cited by 44 publications

References 20 publications

Chemical modification of sarcoplasmic reticulum. Stimulation of Ca2+ release

Chemical modification of sarcoplasmic reticulum. Stimulation of Ca2+ release

Characterization of Calcium, Nucleotide, Phosphate, and Vanadate Bound States by Derivatization of Sarcoplasmic Reticulum ATPase with ThioGlo1

Mechanism of Ca²⁺Transport by Sarcoplasmic Reticulum

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Sarcoplasmic reticulum adenosine triphosphatase: Labeling of an essential lysyl residue with pyridoxal-5′-phosphate

Cited by 44 publications

References 20 publications

Chemical modification of sarcoplasmic reticulum. Stimulation of Ca2+ release

Chemical modification of sarcoplasmic reticulum. Stimulation of Ca2+ release

Characterization of Calcium, Nucleotide, Phosphate, and Vanadate Bound States by Derivatization of Sarcoplasmic Reticulum ATPase with ThioGlo1

Mechanism of Ca2+Transport by Sarcoplasmic Reticulum

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Mechanism of Ca²⁺Transport by Sarcoplasmic Reticulum