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2000 | 47 | 3 | 791-806
Article title

Size, shape and secondary structure of calponin.

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The overall size and shape of the chicken gizzard calponin (CaP) h1 molecule was investigated by dynamic light scattering (DLS) measurements. From the DLS experiments, a z-averaged translational diffusion coefficient is derived (5.75 ± 0.3) × 10-7cm2s-1, which corresponds to a hydrodynamic radius of 3.72 nm for calponin. The frictional ratio (1.8 for the unhydrated molecule and 1.5 for the hydrated one) suggests a pronounced anisotropic structure for the molecule. An ellipsoidal model in length 19.4 nm and with a diameter of 2.6 nm used for hydrodynamic calculations was found to reproduce the DLS experimental data. The evaluation of the secondary structure of CaP h1 from the CD spectra by two independent methods has revealed that it contains, on average, 23% helix, 19% β-strand, 18% β-turns and loops, and 40% of remainder structures. These values are in good agreement with those predicted from the amino-acid sequence. Predictions used for CaP h1 were applied to other isoforms of known sequences and revealed that all calponins share a common secondary structure. Moreover, the predicted structure of the calponin CH domain is identical to that found by X-ray studies of the spectrin, fimbrin and utrophin CH domains.

Physical description
  • Nencki Institute of Experimental Biology, Department of Muscle Biochemistry, Warszawa, Poland
  • Universität Bielefeld, Fakultät für Chemie, Physikalische Chemie 1, Bielefeld, F.R.G.
  • Nencki Institute of Experimental Biology, Department of Muscle Biochemistry, Warszawa, Poland
  • TU Chemnitz, Institut für Physik, Materialforschung und Flüssigkeiten, Chemnitz, F.R.G.
  • Abe, M., Takahashi, K. & Hiwada, K. (1990) Effect of calponin on actin-activated myosin ATPase activity. J. Biochem. (Tokyo) 108, 835-838.
  • Applegate, D., Feng, W., Green, R.S. & Taubman, M.B. (1994) Cloning and expression of a novel acidic calponin isoform from rat aortic vascular smooth muscle. J. Biol. Chem. 269, 10683-10690.
  • Berne, B.J. & Pecora, R. (1976) Dynamic Light Scattering: Applications to Chemistry, Biology, and Physics; 376 p., John Wiley & Sons, Inc., New York.
  • Carugo, K.D., Banuelos, S. & Saraste, M. (1997) Crystal structure of a calponin homology domain. Nat. Struct. Biol. 4, 175-179.
  • Castresana, J. & Saraste, M. (1995) Does Vav bind to F-actin through a CH domain? FEBS Lett. 374, 149-151.
  • Chalovich, J.M. & Pfitzer, G. (1997) Structure and function of the thin filament proteins of smooth muscle; in Cellular Aspects of Smooth Muscle Function (Kao, C.Y. & Carsten, M.E., eds.) pp. 253-287, Cambridge University Press, Cambridge.
  • Czuryło, E.A. (2000) Kalponin: biologicheskie, khimicheskie i strukturnie svoistva [Calponin: biological, chemical and structural properties]. Tsitologiia. 42, 7-18 (in Russian).
  • Czuryło, E.A., Hellweg, T., Eimer, W. & Dąbrowska, R. (1997a) The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations. Biophys. J. 72, 835-842.
  • Czuryło, E.A., Kulikova, N. & Dąbrowska, R. (1997b) Does calponin interact with caldesmon? J. Biol. Chem. 272, 32067-32070.
  • Czuryło, E.A., Venyaminov, S.Y. & Dąbrowska, R. (1993) Studies on secondary structure of caldesmon and its C-terminal fragments. Biochem. J. 293, 363-368.
  • Dąbrowska, R. (1994) Actin and thin filament-associated proteins in smooth muscle; in Airways Smooth Muscle: Biochemical Control of Contraction and Relaxation (Raeburn, D. & Giembycz, M.A., eds.) pp. 31-59, Birkhauser Verlag, Basel.
  • Eimer, W., Niermann, M., Eppe, M.A. & Jockusch, B.M. (1993) Molecular shape of vinculin in aqueous solution. J. Mol. Biol. 229, 146-152.
  • el-Mezgueldi, M. (1996) Calponin. Int. J. Biochem. Cell Biol. 28, 1185-1189.
  • Fujii, T. & Koizumi, Y. (1999) Identification of the binding region of basic calponin on alpha and beta tubulins. J. Biochem. (Tokyo) 125, 869-875.
  • Garcia de la Torre, J. & Bloomfield, V.A. (1981) Hydrodynamic properties of complex, rigid biological macromolecules: Theory and application. Q. Rev. Biophys. 14, 81-139.
  • Gimona, M. & Small, J. V. (1996) Calponin; in Biochemistry of Smooth Muscle Contraction (Barany, M., ed.) pp. 91-103, Academic Press, Inc., San Diego.
  • Gong, B.J., Mabuchi, K., Takahashi, K., Nadal- Ginard, B. & Tao, T. (1993) Characterization of wild type and mutant chicken gizzard alpha calponin expressed in E. coli. J. Biochem. (Tokyo) 114, 453-456.
  • Haeberle, J.R. (1994) Calponin decreases the rate of cross-bridge cycling and increases maximum force production by smooth muscle myosin in an in vitro motility assay. J. Biol. Chem. 269, 12424-12431.
  • Hanein, D., Volkmann, N., Goldsmith, S., Michon, A.M., Lehman, W., Craig, R., DeRosier, D., Almo, S. & Matsudaira, P. (1998) An atomic model of fimbrin binding to F-actin and its implications for filament crosslinking and regulation. Nat. Struct. Biol. 5, 787-792.
  • Hennessey, J.P., Jr. & Johnson, W.C., Jr. (1981) Information content in the circular dichroism of proteins. Biochemistry 20, 1085-1094.
  • Hodgkinson, J.L., el-Mezgueldi, M., Craig, R., Vibert, P., Marston, S.B. & Lehman, W. (1997) 3-D Image reconstruction of reconstituted smooth muscle thin filaments containing calponin: Visualization of interactions between F-actin and calponin. J. Mol. Biol. 273, 150-159.
  • Horowitz, A., Menice, C.B., Laporte, R. & Morgan, K.G. (1996) Mechanisms of smooth muscle contraction. Physiol. Rev. 76, 967-1003.
  • Jin, J.P., Walsh, M.P., Resek, M.E. & McMartin, G.A. (1996) Expression and epitopic conservation of calponin in different smooth muscles and during development. Biochem. Cell Biol. 74, 187-196.
  • Keep, N.H., Norwood, F.L., Moores, C.A., Winder, S.J. & Kendrick-Jones, J. (1999) The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin. J. Mol. Biol. 285, 1257-1264.
  • Kołakowski, J., Makuch, R., Stępkowski, D. & Dąbrowska, R. (1995) Interaction of calponin with actin and its functional implications. Biochem. J. 306, 199-204.
  • Koppel, D.E. (1972) Analysis of macromolecular polydispersity in intensity correlation spectroscopy: The method of cumulants. J. Chem. Phys. 57, 4814-4820.
  • Lazard, D., Sastre, X., Frid, M.G., Glukhova, M.A., Thiery, J.P. & Koteliansky, V.E. (1993) Expression of smooth muscle-specific proteins in myoepithelium and stromal myofibroblasts of normal and malignant human breast tissue. Proc. Natl. Acad. Sci. U. S. A. 90, 999-1003.
  • Leinweber, B., Tang, J.X., Stafford, W.F. & Chalovich, J.M. (1999a) Calponin interaction with alpha-actinin-actin: Evidence for a structural role for calponin. Biophys. J. 77, 3208-3217.
  • Leinweber, B.D., Leavis, P.C., Grabarek, Z., Wang, C.A. & Morgan, K.G. (1999b) Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins. Biochem. J. 344, 117-123.
  • Lim, V.I. (1978) Polypeptide chain folding through a highly helical intermediate as a general principle of globular protein structure formation. FEBS Lett. 89, 10-14.
  • Lu, F.W., Freedman, M.V. & Chalovich, J.M. (1995) Characterization of calponin binding to actin. Biochemistry 34, 11864-11871.
  • Mabuchi, K., Li, Y., Tao, T. & Wang, C.L. (1996) Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle. J. Muscle Res. Cell Motil. 17, 243- 260.
  • Makuch, R., Birukov, K., Shirinsky, V. & Dąbrowska, R. (1991) Functional interrelationship between calponin and caldesmon. Biochem. J. 280, 33-38.
  • Marston, S.B. (1991) Properties of calponin isolated from sheep aorta thin filaments. FEBS Lett. 292, 179-182.
  • Menice, C.B., Hulvershorn, J., Adam, L.P., Wang, C.A. & Morgan, K.G. (1997) Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle. J. Biol. Chem. 272, 25157-25161.
  • Mezgueldi, M., Fattoum, A., Derancourt, J. & Kassab, R. (1992) Mapping of the functional domains in the amino-terminal region of calponin. J. Biol. Chem. 267, 15943-15951.
  • Miano, J.M., Krahe, R., Garcia, E., Elliott, J.M. & Olson, E.N. (1997) Expression, genomic structure and high resolution mapping to 19p13.2 of the human smooth muscle cell calponin gene. Gene 197, 215-224.
  • Nigam, R., Triggle, C.R. & Jin, J.P. (1998) h1- and h2-calponins are not essential for norepinephrine- or sodium fluoride-induced contraction of rat aortic smooth muscle. J. Muscle Res. Cell Motil. 19, 695-703.
  • North, A.J., Gimona, M., Cross, R.A. & Small, J.V. (1994) Calponin is localised in both the contractile apparatus and the cytoskeleton of smooth muscle cells. J. Cell Sci. 107, 437- 444.
  • Patkowski, A., Eimer, W., Schneider, G., Jokusch, B.M. & Dorfmüller, T. (1990a) The molecular dimensions of G-actin in solution as studied by dynamic light scattering. Biopolymers 30, 1281-1287.
  • Patkowski, A., Seils, J., Hinssen, H. & Dorfmüller, T. (1990b) Size, shape parameters, and Ca2+-induced conformational change of the gelsolin molecule: A dynamic light scattering study. Biopolymers 30, 427-435.
  • Provencher, S.W. (1982a) A constrained regularization method for inverting data represented by linear algebraic or integral equations. Comput. Phys. Commun. 27, 213-217.
  • Provencher, S.W. (1982b) Contin: A general purpose constrained regularization program for inverting noisy linear algebraic and integral equations. Comput. Phys. Commun. 27, 229-242.
  • Provencher, S.W. & Glöckner, J. (1981) Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20, 33-37.
  • Ptitsyn, O.B. & Finkelstein, A.V. (1983) Theory of protein secondary structure and algorithm of its prediction. Biopolymers 22, 15-25.
  • Rost, B. & Sander, C. (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 55-72.
  • Rost, B., Sander, C. & Schneider, R. (1994) Redefining the goals of protein secondary structure prediction. J. Mol. Biol. 235, 13-26.
  • Rotne, J. & Prager, S. (1969) Vibrational treatment of hydrodynamic interaction in polymer. J. Chem. Phys. 50, 4831-4837.
  • Shirinsky, V.P., Biryukov, K.G., Hettasch, J.M. & Sellers, J.R. (1992) Inhibition of the relative movement of actin and myosin by caldesmon and calponin. J. Biol. Chem. 267, 15886- 15892.
  • Small, J.V. & Gimona, M. (1998) The cytoskeleton of the vertebrate smooth muscle cell. Acta Physiol. Scand. 164, 341-348.
  • Stafford, W.F., Mabuchi, K., Takahashi, K. & Tao, T. (1995) Physical characterization of calponin. A circular dichroism, analytical ultracentrifuge, and electron microscopy study. J. Biol. Chem. 270, 10576-10579.
  • Stradal, T., Kranewitter, W., Winder, S.J. & Gimona, M. (1998) CH domains revisited. FEBS Lett. 431, 134-137.
  • Strasser, P., Gimona, M., Moessler, H., Herzog, M. & Small, J.V. (1993) Mammalian calponin. Identification and expression of genetic variants. FEBS Lett. 330, 13-18.
  • Szymanski, P.T. & Goyal, R.K. (1999) Calponin binds to the 20-kilodalton regulatory light chain of myosin. Biochemistry 38, 3778-3784.
  • Szymanski, P.T. & Tao, T. (1993) Interaction between calponin and smooth muscle myosin. FEBS Lett. 334, 379-382.
  • Szymanski, P.T. & Tao, T. (1997) Localization of protein regions involved in the interaction between calponin and myosin. J. Biol. Chem. 272, 11142-11146.
  • Takahashi, K., Hiwada, K. & Kokubu, T. (1986) Isolation and characterization of a 34000-dalton calmodulin- and F- actin-binding protein from chicken gizzard smooth muscle. Biochem. Biophys. Res. Commun. 141, 20-26.
  • Takahashi, K., Hiwada, K. & Kokubu, T. (1988) Vascular smooth muscle calponin. A novel troponin T-like protein. Hypertension 11, 620-626.
  • Takahashi, K. & Nadal-Ginard, B. (1991) Molecular cloning and sequence analysis of smooth muscle calponin. J. Biol. Chem. 266, 13284- 13288.
  • Takeuchi, K., Takahashi, K., Abe, M., Nishida, W., Hiwada, K., Nabeya, T. & Maruyama, K. (1991) Co-localization of immunoreactive forms of calponin with actin cytoskeleton in platelets, fibroblasts, and vascular smooth muscle. J. Biochem. (Tokyo) 109, 311-316.
  • Tang, D.C., Kang, H.M., Jin, J.P., Fraser, E.D. & Walsh, M.P. (1996) Structure-function relations of smooth muscle calponin. The critical role of serine 175. J. Biol. Chem. 271, 8605- 8611.
  • Trabelsi-Terzidis, H., Fattoum, A., Represa, A., Dessi, F., Ben-Ari, Y. & Der Terrossian, E. (1995) Expression of an acidic isoform of calponin in rat brain: Western blots on one- or two-dimensional gels and immunolocalization in cultured cells. Biochem. J. 306, 211-215.
  • Vancompernolle, K., Gimona, M., Herzog, M., Van Damme, J., Vandekerckhove, J. & Small, V. (1990) Isolation and sequence of a tropomyosin-binding fragment of turkey gizzard calponin. FEBS Lett. 274, 146-150.
  • Venyaminov, S., Baikalov, I.A., Shen, Z.M., Wu, C.S. & Yang, J.T. (1993) Circular dichroic analysis of denatured proteins: Inclusion of denatured proteins in the reference set. Anal. Biochem. 214, 17-24.
  • Wang, P. & Gusev, N.B. (1996) Interaction of smooth muscle calponin and desmin. FEBS Lett. 392, 255-258.
  • Wills, F.L., McCubbin, W.D. & Kay, C.M. (1993) Characterization of the smooth muscle calponin and calmodulin complex. Biochemistry 32, 2321-2328.
  • Winder, S.J., Allen, B.G., Clement-Chomienne, O. & Walsh, M.P. (1998) Regulation of smooth muscle actin-myosin interaction and force by calponin. Acta Physiol. Scand. 164, 415-426.
  • Winder, S.J. & Walsh, M.P. (1990a) Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. J. Biol. Chem. 265, 10148-10155.
  • Winder, S.J. & Walsh, M.P. (1990b) Structural and functional characterization of calponin fragments. Biochem. Int. 22, 335-341.
  • Yang, J.Y., Wu, C.S.C. & Martinez, H.M. (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269.
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