Preferences help
enabled [disable] Abstract
Number of results
2000 | 47 | 4 | 1019-1026
Article title

Motifs of the caldesmon family.

Title variants
Languages of publication
Seven highly conserved regions were found in caldesmon molecules from various sources using the multiple sequence alignment method. Their localization coincides with regions where the binding sites to other proteins were postulated. Less conserved and highly divergent regions of the sequences are described as well. These results could refine the planning of caldesmon gene manipulations and accelerate the precise localization of binding sites in the caldesmon molecule and, as a consequence, this could help to elucidate its function in smooth muscle contraction.
Physical description
  • Nencki Institute of Experimental Biology, Department of Muscle Biochemistry, Warszawa, Poland
  • Bartegi, A., Fattoum, A., Derancourt, J. & Kassab, R. (1990) Characterization of the carboxyl- terminal 10-kDa cyanogen bromide fragment of caldesmon as an actin-calmodulin-binding region. J. Biol. Chem. 265, 15231-15238.
  • Chalovich, J.M., Bryan, J., Benson, C.E. & Velaz, L. (1992) Localization and characterization of a 7.3-kDa region of caldesmon which reversibly inhibits actomyosin ATPase activity. J. Biol. Chem. 267, 16644-16650.
  • 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, U.K.
  • Chalovich, J.M., Sen, A., Resetar, A., Leinweber, B., Fredricksen, R.S., Lu, F. & Chen, Y.D. (1998) Caldesmon: Binding to actin and myosin and effects on elementary steps in the ATPase cycle. Acta Physiol. Scand. 164, 427-435.
  • Combet, C., Blanchet, C., Geourjon, C. & Deléage, G. (2000) NPS@: Network Protein Sequence Analysis. Trends Biochem. Sci. 25, 147-150.
  • Czuryło, E.A., Emelyanenko, V.I., Permyakov, E.A. & Dąbrowska, R. (1991) Spectrofluorimetric studies on C-terminal 34 kDa fragment of caldesmon. Biophys. Chem. 40, 181-188.
  • 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. & Dąbrowska, R. (1993) Studies on secondary structure of caldesmon and its C-terminal fragments. Biochem. J. 293, 363-368.
  • Fraser, I.D., Copeland, O., Bing, W. & Marston, S.B. (1997) The inhibitory complex of smooth muscle caldesmon with actin and tropomyosin involves three interacting segments of the C-terminal domain 4. Biochemistry 36, 5483-5492.
  • Gałązkiewicz, B., Mossakowska, M., Osińska, H. & Dąbrowska, R. (1985) Polymerization of G-actin by caldesmon. FEBS Lett. 184, 144-149.
  • Gao, Y., Patchell, V.B., Huber, P.A., Copeland, O., El-Mezgueldi, M., Fattoum, A., Calas, B., Thorsted, P.B., Marston, S.B. & Levine, B.A. (1999) The interface between caldesmon domain 4b and subdomain 1 of actin studied by nuclear magnetic resonance spectroscopy. Biochemistry 38, 15459-15469.
  • Hall, T.A. (1999) BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41, 95-98.
  • Haruna, M., Hayashi, K., Yano, H., Takeuchi, O. & Sobue, K. (1993) Common structural and expressional properties of vertebrate caldesmon genes. Biochem. Biophys. Res. Commun. 197, 145-153.
  • Hayashi, K., Kanda, K., Kimizuka, F., Kato, I. & Sobue, K. (1989) Primary structure and functional expression of h-caldesmon complementary DNA. Biochem. Biophys. Res. Commun. 164, 503-511.
  • Hayashi, K., Yano, H., Hashida, T., Takeuchi, R., Takeda, O., Asada, K., Takahashi, E., Kato, I. & Sobue, K. (1992) Genomic structure of the human caldesmon gene. Proc. Natl. Acad. Sci. U.S.A. 89, 12122-12126.
  • Higgins, D.G., Thompson, J.D. & Gibson, T.J. (1996) Using CLUSTAL for multiple sequence alignments. Methods Enzymol. 266, 383-402.
  • Huber, P.A. (1997) Caldesmon. Int. J. Biochem. Cell Biol. 29, 1047-1051.
  • Huber, P.A.J., Gao, Y., Fraser, I.D.C., Copeland, O., el-Mezgueldi, M., Slatter, D.A., Keane, N.E., Marston, S.B. & Levine, B.A. (1998) Structure-activity studies of the regulatory interaction of the 10 kilodalton C-terminal fragment of caldesmon with actin and the effect of mutation of caldesmon residues 691-696. Biochemistry 37, 2314-2326.
  • Lee, Y.H., Gallant, C., Guo, H., Li, Y., Wang, C.A. & Morgan, K.G. (2000) Regulation of vascular smooth muscle tone by N-terminal region of caldesmon. Possible role of tethering actin to myosin. J. Biol. Chem. 275, 3213-3220.
  • Lehman, W., Craig, R., Lui, J. & Moody, C. (1989) Caldesmon and the structure of smooth muscle thin filaments: Immunolocalization of caldesmon on thin filaments. J. Muscle Res. Cell Motil. 10, 101-112.
  • Leszyk, J., Mornet, D., Audemard, E. & Collins, J.H. (1989) Amino acid sequence of a 15 kilodalton actin-binding fragment of turkey gizzard caldesmon: Similarity with dystrophin, tropomyosin and the tropomyosin-binding region of troponin T. Biochem. Biophys. Res. Commun. 160, 210-216.
  • Li, Y., Zhuang, S., Guo, H., Mabuchi, K., Lu, R.C. & Wang, C.A. (2000) The major myosin-binding site of caldesmon resides near its N-terminal extreme. J. Biol. Chem. 275, 10989-10994.
  • Mabuchi, K. & Wang, C.L. (1991) Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin. J. Muscle Res. Cell. Motil. 12, 145-151.
  • Marston, S. & Huber, P. (1996) Caldesmon; in Biochemistry of Smooth Muscle Contraction (Barany, M., ed.) pp. 77-90, Academic Press, Inc., San Diego.
  • Marston, S., Burton, D., Copeland, O., Fraser, I., Gao, Y., Hodgkinson, J., Huber, P., Levine, B., el-Mezgueldi, M. & Notarianni, G. (1998) Structural interactions between actin, tropomyosin, caldesmon and calcium binding protein and the regulation of smooth muscle thin filaments. Acta Physiol. Scand. 164, 401-414.
  • Mezgueldi, M., Derancourt, J., Calas, B., Kassab, R. & Fattoum, A. (1994) Precise identification of the regulatory F-actin- and calmodulin-binding sequences in the 10-kDa carboxyl-terminal domain of caldesmon. J. Biol. Chem. 269, 12824-12832.
  • Mornet, D., Audemard, E. & Derancourt, J. (1988) Identification of a 15 kilodalton actin binding region on gizzard caldesmon probed by chemical cross-linking. Biochem. Biophys. Res. Commun. 154, 564-571.
  • Rost, B., Sander, C. & Schneider, R. (1994) PHD an automatic mail server for protein secondary structure prediction. Comput. Appl. Biosci. 10, 53-60.
  • Sobue, K., Muramoto, Y., Fujita, M. & Kakiuchi, S. (1981) Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc. Natl. Acad. Sci. U.S.A. 78, 5652-5655.
  • Sobue, K. & Sellers, J.R. (1991) Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems. J. Biol. Chem. 266, 12115-12118.
  • Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
  • Wang, C.L. (1988) Photocrosslinking of calmodulin and/or actin to chicken gizzard caldesmon. Biochem. Biophys. Res. Commun. 156, 1033-1038.
  • Wang, C.L., Chalovich, J.M., Graceffa, P., Lu, R.C., Mabuchi, K. & Stafford, W.F. (1991a) A long helix from the central region of smooth muscle caldesmon. J. Biol. Chem. 266, 13958- 13963.
  • Wang, C.L., Wang, L.W., Xu, S.A., Lu, R.C., Saavedra-Alanis, V. & Bryan, J. (1991b) Localization of the calmodulin- and the actin-binding sites of caldesmon. J. Biol. Chem. 266, 9166-9172.
  • Wang, E. & Wang, C.L. (1996) (i, i + 4) Ion pairs stabilize helical peptides derived from smooth muscle caldesmon. Arch. Biochem. Biophys. 329, 156-162.
  • Wang, Z., Jiang, H., Yang, Z.Q. & Chacko, S. (1997) Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon-mediated inhibition of actin filament velocity. Proc. Natl. Acad. Sci. U.S.A. 94, 11899-11904.
Document Type
Publication order reference
YADDA identifier
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.