Interaction of smooth muscle caldesmon with S‐100 protein

Skripnikova, Elena; Gusev, Nikolai B.

doi:10.1016/0014-5793(89)81577-7

Cited by 46 publications

(37 citation statements)

References 23 publications

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“…5), tropomyosin (Fig. 4,[19]) and calmodulin [5]. These results indicate that caldesmon expressed in a bacterial cell refolds into its native state and remains stable under the harsh conditions used for its subsequent purification (95°C [14], pH 3 [3]).…”

Section: Expressed Wild Type Caldesmon Is Fully Functionalmentioning

confidence: 95%

The functional properties of full length and mutant chicken gizzard smooth muscle caldesmon expressed in Escherichia coli

Redwood¹,

Marston²,

Bryan

et al. 1990

FEBS Letters

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Wild type chicken gizzard caldesmon (756 amino acids) was expressed in a T7 RNA polymerase-based bacterial expression system at a yield of 1 mg pure caldesmon per litre bacterial culture. A mutant composed of amino acids l-578 was also constructed and expressed. The wild type and mutant caldesmon were purified and compared with native chicken gizzard caldesmon. Native and wild type expressed caldesmon were indistinguishable in assays for inhibition of actin-tropomyosin activation of myosin ATPase, reversal of inhibition by Caz+-cahnodulin and binding to actin, actin-tropomyosin, Ca2+-calmodulin, tropomyosin and myosin. The mutant missing the C-terminal 178 amino acids had no inhibitory effect and did not bind to actin or Ca*+-calmodulin. It bound to tropomyosin with a 5-fold reduced affinity and to myosin with a greater than IO-fold reduced affinity.

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Section: Expressed Wild Type Caldesmon Is Fully Functionalmentioning

confidence: 95%

The functional properties of full length and mutant chicken gizzard smooth muscle caldesmon expressed in Escherichia coli

Redwood¹,

Marston²,

Bryan

et al. 1990

FEBS Letters

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“…Caldesmon interacts with a number of calcium-binding proteins such as calmodulin [1][2][3], S-100 protein [4,5], caltropin [6] and troponin C [7]. Of all these proteins, calmodulin seems to be the most probable regulator of caldesmon function in smooth muscle [1][2][3].…”

Section: Introductionmentioning

confidence: 99%

Interaction of smooth muscle caldesmon with calmodulin mutants

Медведева

Bushueva²,

Shirinsky³

et al. 1995

FEBS Letters

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The interaction of avian smooth muscle caldesmon with calmodulin (CAM) was investigated by studying the ability of selected mutant calmodulins to induce fluorescence changes in caldesmon. Different types of CaM mutants were used including point charge mutants, cluster mutations, and mutations which alter the calcium binding of CaM. The caldesmon binding properties were only slightly affected by E84K-CaM or by the double mutation E84Q/E120Q-CaM. Affinity of calmodulin to caldesmon was decreased 2-4 times by point mutation G33V-CaM, double mutation E841(dEI20K-CaM, deletion of residues 82-84, and by cluster mutations DEEll8-120-->KKK or EEE82-84--~KKK. Mutations of the first (E31A-CaM) and the second (E67A-CaM) calcium binding sites reduced the affinity of calmodulin to caldesmon by at least 5-fold; in addition these calmodulin mutants exhibited smaller changes in the fluorescence spectra of caldesmon. Simultaneous mutation of the two negatively charged clusters of calmodulin EEE82-84--~ KKK and DEEll8-120 --> KKK resulted in a more than 15-fold decrease in the affinity of calmodulin for caldesmon. The data indicate that charged and uncharged amino acids in both halves of CaM play an important role in the binding of calmodulin to caldesmon, and that Ca 2+ binding must be maintained in the amino-terminal sites for maximal interaction with caldesmon.

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“…Identification of the in vivo S100B target proteins is essential for the determination of the exact contribution of the protein to cell functions. Several putative S100B target proteins have already been characterized, including cytoskeleton-associated proteins (15)(16)(17)(18)(19)(20), nuclear protein kinase (21), and nuclear transcription factors (22,23). In all cases, these interactions depend on the Ca 2ϩ -bound S100B conformation.…”

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confidence: 99%

S100A6 and S100A11 Are Specific Targets of the Calcium- and Zinc-binding S100B Protein in Vivo

Deloulme¹,

Assard²,

Mbele³

et al. 2000

Journal of Biological Chemistry

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In solution, S100B protein is a noncovalent homodimer composed of two subunits associated in an antiparallel manner. Upon calcium binding, the conformation of S100B changes dramatically, leading to the exposure of hydrophobic residues at the surface of S100B. The residues in the C-terminal domain of S100B encompassing Phe 87 and Phe 88 have been implicated in interaction with target proteins. In this study, we used two-hybrid technology to identify specific S100B target proteins. Using S100B as bait, we identify S100A6 and S100A11 as specific targets for S100B. S100A1, the closest homologue of S100B, is capable of interaction with S100B but does not interact with S100A6 or S100A11. S100B, S100A6, and S100A11 isoforms are co-regulated and co-localized in astrocytoma U373 cells. Furthermore, co-immunoprecipitation experiments demonstrated that Ca 2؉ /Zn 2؉ stabilizes S100B-S100A6 and S100B-S100A11 heterocomplexes. Deletion of the C-terminal domain or mutation of Phe 87 and Phe 88 residues has no effect on S100B homodimerization and heterodimerization with S100A1 but drastically decreases interaction between S100B and S100A6 or S100A11. Our data suggest that the interaction between S100B and S100A6 or S100A11 should not be viewed as a typical S100 heterodimerization but rather as a model of interaction between S100B and target proteins.

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Interaction of smooth muscle caldesmon with S‐100 protein

Cited by 46 publications

References 23 publications

The functional properties of full length and mutant chicken gizzard smooth muscle caldesmon expressed in Escherichia coli

The functional properties of full length and mutant chicken gizzard smooth muscle caldesmon expressed in Escherichia coli

Interaction of smooth muscle caldesmon with calmodulin mutants

S100A6 and S100A11 Are Specific Targets of the Calcium- and Zinc-binding S100B Protein in Vivo

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