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2000 | 47 | 4 |

Tytuł artykułu

Motifs of the caldesmon family

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
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.

Wydawca

-

Rocznik

Tom

47

Numer

4

Opis fizyczny

p.1019-1026,fig.,ref.

Twórcy

  • Nencki Institute of Experimental Biology, L.Pasteura 3, 02-093 Warsaw, Poland

Bibliografia

  • 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 revers- ibly 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 myo- sin and effects on elementary steps in the ATPase cycle. Acta Physiol. Scand. 164, 427-435.
  • Combet, C., Blanchet, C., Geourjon, C. & Deleage, 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) Spectrofluo- rimetric 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 hydrody- namic model calculations. Biophys. J. 72, 835-842.
  • Czuryło, E.A., Kulikova, N. & Dąbrowska, R. (1997b) Does calponin interact with caldes- mon? J. Biol. Chem. 272, 32067-32070.
  • Czuryło, E.A., Venyaminov, S. & Dąbrowska, R. (1993) Studies on secondary structure of cal- desmon 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-ac- tin 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 caldes- mon 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.
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  • 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. CellMotil. 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 dystro- phin, tropomyosin and the tropo- myosin-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-bind- ing 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, tropo- myosin, 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-bind- ing 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. 266,13958­13963.
  • 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-bind- ing 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-me- diated inhibition of actin filament velocity. Proc. Natl. Acad. Sci. U.S.A. 94,11899-11904.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-f621339e-9987-458e-bfe4-50b1b715f8fb
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