Calcium binding to recoverin: implications for secondary structure and membrane association

Johnson, W. Curtis; Palczewski, Krzysztof; Gorczyca, Wojciech; Riazance‐Lawrence, Jeannine H.; Witkowska, Danuta; Polans, Arthur S.

doi:10.1016/s0167-4838(97)00091-5

Cited by 25 publications

(15 citation statements)

References 44 publications

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“…However, EF-hand proteins undergo conformational transitions upon binding with Ca 2ϩ that often increase their ␣ helical content, a conformation conducive for binding dsRNA (21)(22)(23). We therefore reasoned that Ca 2ϩ may be required by VILIP to assume a secondary structure that would allow dsRNA binding.…”

Section: Resultsmentioning

confidence: 99%

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Visinin-like Protein (VILIP) Is a Neuron-specific Calcium-dependent Double-stranded RNA-binding Protein

Mathisen

Johnson

Kawczak

et al. 1999

Journal of Biological Chemistry

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Double-stranded RNA-binding proteins function in regulating the stability, translation, and localization of specific mRNAs. In this study, we have demonstrated that the neuron-specific, calcium-binding protein, visinin-like protein (VILIP) contains one double-stranded RNA-binding domain, a protein motif conserved among many double-stranded RNA-binding proteins. We showed that VILIP can specifically bind doublestranded RNA, and this interaction specifically requires the presence of calcium. Mobility shift studies indicated that VILIP binds double-stranded RNA as a single protein-RNA complex with an apparent equilibrium dissociation constant of 9.0 ؋ 10 ؊6 M. To our knowledge, VILIP is the first double-stranded RNA-binding protein shown to be calcium-dependent. Furthermore, VILIP specifically binds the 3-untranslated region of the neurotrophin receptor, trkB, an mRNA localized to hippocampal dendrites in an activity-dependent manner. Given that VILIP is also expressed in the hippocampus, these data suggest that VILIP may employ a novel, calcium-dependent mechanism to regulate its binding to important localized mRNAs in the central nervous system.

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Section: Resultsmentioning

confidence: 99%

“…(24). Furthermore, Ca 2ϩ binding of recoverin, another EF-hand protein, increases recoverin ␣ helical content (22). RNA binding has been shown to be mediated by ␣ helical-enriched proteins, and ␣ helices have been demonstrated for the structure of the dsRNA-binding domain (27)(28)(29)(30).…”

Section: Discussionmentioning

confidence: 99%

Visinin-like Protein (VILIP) Is a Neuron-specific Calcium-dependent Double-stranded RNA-binding Protein

Mathisen

Johnson

Kawczak

et al. 1999

Journal of Biological Chemistry

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“…Concentrations of purified recoverin and calmodulin were determined spectrophotometrically assuming ε 280 of 27,500 and 3,030 M −1 cm −1 , respectively (Wallace et al, 1983; Johnson et al, 1997). Concentrations of GST–RK constructs were measured using Bradford protein assay (Bio-Rad Laboratories) calibrated with bovine serum albumin.…”

Section: Methodsmentioning

confidence: 99%

Synergetic Effect of Recoverin and Calmodulin on Regulation of Rhodopsin Kinase

Grigoriev¹,

Senin²,

Тихомирова³

et al. 2012

Front. Mol. Neurosci.

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Phosphorylation of photoactivated rhodopsin by rhodopsin kinase (RK or GRK1), a first step of the phototransduction cascade turnoff, is under the control of Ca2+/recoverin. Here, we demonstrate that calmodulin, a ubiquitous Ca2+-sensor, can inhibit RK, though less effectively than recoverin does. We have utilized the surface plasmon resonance technology to map the calmodulin binding site in the RK molecule. Calmodulin does not interact with the recoverin-binding site within amino acid residues M1-S25 of the enzyme. Instead, the high affinity calmodulin binding site is localized within a stretch of amino acid residues V150-K175 in the N-terminal regulatory region of RK. Moreover, the inhibitory effect of calmodulin and recoverin on RK activity is synergetic, which is in agreement with the existence of separate binding sites for each Ca2+-sensing protein. The synergetic inhibition of RK by both Ca2+-sensors occurs over a broader range of Ca2+-concentration than by recoverin alone, indicating increased Ca2+-sensitivity of RK regulation in the presence of both Ca2+-sensors. Taken together, our data suggest that RK regulation by calmodulin in photoreceptor cells could complement the well-known inhibitory effect of recoverin on RK.

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“…The shoulders at 1630 cm À1 and ;1678 cm À1 can been assigned to b-sheet and b-turn structures of recoverin, respectively (40,51,76,82). Indeed, Johnson et al (83) have shown that recoverin in the presence of 1 mM calcium contains 11% parallel and antiparallel b-sheet and 13% of b-turn. In addition, the NMR analysis of the secondary structure of recoverin revealed the presence of 11 helical segments and two pairs of antiparallel b-sheets (31).…”

Section: Monitoring Of the Adsorption Of Recoverin Onto Dmpc Monolayementioning

confidence: 99%

Determination of the Contribution of the Myristoyl Group and Hydrophobic Amino Acids of Recoverin on its Dynamics of Binding to Lipid Monolayers

Desmeules

Penney

Desbat

et al. 2007

Biophysical Journal

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It has been postulated that myristoylation of peripheral proteins would facilitate their binding to membranes. However, the exact involvement of this lipid modification in membrane binding is still a matter of debate. Proteins containing a Ca(2+)-myristoyl switch where the extrusion of their myristoyl group is dependent on calcium binding is best illustrated by the Ca(2+)-binding recoverin, which is present in retinal rod cells. The parameters responsible for the modulation of the membrane binding of recoverin are still largely unknown. This study was thus performed to determine the involvement of different parameters on recoverin membrane binding. We have used surface pressure measurements and PM-IRRAS spectroscopy to monitor the adsorption of myristoylated and nonmyristoylated recoverin onto phospholipid monolayers in the presence and absence of calcium. The adsorption curves have shown that the myristoyl group and hydrophobic residues of myristoylated recoverin strongly accelerate membrane binding in the presence of calcium. In the case of nonmyristoylated recoverin in the presence of calcium, hydrophobic residues alone are responsible for its much faster monolayer binding than myristoylated and nonmyristoylated recoverin in the absence of calcium. The infrared spectra revealed that myristoylated and nonmyristoylated recoverin behave very different upon adsorption onto phospholipid monolayers. Indeed, PM-IRRAS spectra indicated that the myristoyl group allows a proper orientation and organization as well as faster and stronger binding of myristoylated recoverin to lipid monolayers compared to nonmyristoylated recoverin. Simulations of the spectra have allowed us to postulate that nonmyristoylated recoverin changes conformation and becomes hydrated at large extents of adsorption as well as to estimate the orientation of myristoylated recoverin with respect to the monolayer plane. In addition, adsorption measurements and electrophoresis of trypsin-treated myristoylated recoverin in the presence of zinc or calcium demonstrated that recoverin has a different conformation but a similar extent of monolayer binding in the presence of such ions.

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Calcium binding to recoverin: implications for secondary structure and membrane association

Cited by 25 publications

References 44 publications

Visinin-like Protein (VILIP) Is a Neuron-specific Calcium-dependent Double-stranded RNA-binding Protein

Visinin-like Protein (VILIP) Is a Neuron-specific Calcium-dependent Double-stranded RNA-binding Protein

Synergetic Effect of Recoverin and Calmodulin on Regulation of Rhodopsin Kinase

Determination of the Contribution of the Myristoyl Group and Hydrophobic Amino Acids of Recoverin on its Dynamics of Binding to Lipid Monolayers

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