Artículos de revistas
Mapping Contacts Between Regulatory Domains Of Skeletal Muscle Tnc And Tni By Analyses Of Single-chain Chimeras
Registro en:
Febs Journal. , v. 272, n. 3, p. 779 - 790, 2005.
1742464X
10.1111/j.1742-4658.2004.04515.x
2-s2.0-13444253928
Autor
Tiroli A.O.
Tasic L.
Oliveira C.L.P.
Bloch Jr. C.
Torriani I.
Farah C.S.
Ramos C.H.I.
Institución
Resumen
The troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnI-TnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 1-91 of TnC linked to residues 98-182 or 98-147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148-182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148-182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114-137. 272 3 779 790 Farah, C.S., Reinach, F.C., The troponin complex and regulation of muscle contraction (1995) FASEB J, 9, pp. 755-767 Gordon, A.M., Homsher, E., Regnier, M., Regulation of contraction in striated muscle (2000) Physiol Rev, 80, pp. 853-924 Potter, J.D., Gergely, J., The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase (1975) J Biol Chem, 250, pp. 4628-4633 Zot, H.J., Potter, J.D., A structural role for the Ca2+-Mg2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils (1982) J Biol Chem, 257, pp. 7678-7683 Syska, H., Wilkinson, J.M., Grand, R.J.A., Perry, S.V., The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit (1976) Biochem J, 153, pp. 375-387 Herzberg, O., James, M.N., Structure of the calcium regulatory muscle protein troponin-C at 28 A resolution (1985) Nature, 313, pp. 653-659 Johnson, J.D., Charlton, S.C., Potter, J.D., A fluorescence stopped flow analysis of Ca2+ exchange with troponin C (1979) J Biol Chem, 254, pp. 3497-3502 Li, M.X., Chandra, M., Pearlstone, J.R., Racher, K.I., Trigo-Gonzalez, G., Borgford, T., Kay, C.M., Smillie, L.B., Properties of isolated recombinant N and C domains of chicken troponin C (1994) Biochemistry, 33, pp. 917-925 Gagne, S.M., Tsuda, S., Li, M.X., Smillie, L.B., Sykes, B.D., Structures of the troponin C regulatory domains in the apo and calcium-saturated states (1995) Nat Struct Biol, 2, pp. 784-789 Farah, C.S., Miyamoto, C.A., Ramos, C.H.I., Silva, A.C.R., Quaggio, R.B., Fujimori, K., Smillie, L.B., Reinach, F.C., Structural and regulatory functions of the NH2- and COOH-terminal regions of skeletal muscle troponin I (1994) J Biol Chem, 269, pp. 5230-5240 Kobayashi, T., Tao, T., Gergely, J., Collins, J.H., Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants (1994) J Biol Chem, 269, pp. 5725-5729 McKay, R.T., Tripet, B.P., Hodges, R.S., Sykes, B.D., Interaction of the second binding region of troponin I with the regulatory domain of skeletal muscle troponin C as determined by NMR spectroscopy (1997) J Biol Chem, 272, pp. 28494-28500 Pearlstone, J.R., Sykes, B.D., Smillie, L.B., Interactions of structural C and regulatory N domains of troponin C with repeated sequence motifs in troponin I (1997) Biochemistry, 36, pp. 7601-7606 Takeda, S., Kobayashi, T., Taniguchi, H., Hayashi, H., Maeda, Y., Structural and functional domains of the troponin complex revealed by limited digestion (1997) Eur J Biochem, 246, pp. 611-617 Tripet, B., VanEik, J.E., Hodges, R.S., Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca 2+-dependent regulation of muscle contraction (1997) J Mol Biol, 271, pp. 728-750 Ramos, C.H.I., Mapping subdomains in the C-terminal region of troponin I involved in its binding to troponin C and to thin filament (1999) J Biol Chem, 274, pp. 18189-18195 Olah, G.A., Trewhella, J., A model structure of the muscle protein complex 4Ca2+.troponin C.troponin I derived from small-angle scattering data: Implications for regulation (1994) Biochemistry, 33, pp. 12800-12806 Stone, D.B., Timmins, P.A., Schneider, D.K., Krylova, I., Ramos, C.H.I., Reinach, F.C., Mendelson, R.A., The effect of regulatory Ca2+ on the in situ structures of troponin C and troponin I: A neutron scattering study (1998) J Mol Biol, 281, pp. 689-704 McKay, R.T., Pearlstone, J.R., Corson, D.C., Gagne, S.M., Smillie, L.B., Sykes, B.D., Structure and interaction site of the regulatory domain of troponin-C when complexed with the 96-148 region of troponin-I (1998) Biochemistry, 37, pp. 12419-12430 Takeda, S., Yamashita, A., Maeda, K., Maeda, Y., Structure of the core domain of human cardiac troponin in the Ca (2+)-saturated form (2003) Nature, 424, pp. 35-41 Ramos, C.H.I., Lima Jr., M.V., Silva, S.L., Borin, P.F.L., Régis, W.C.B., Santoro, M.M., Stability and folding studies of the N-domain of troponin C. Evidence for the formation of an intermediate (2004) Arch Biochem Biophys, 427, pp. 135-142 Svergun, D.I., Barberato, C., Koch, M.H.J., CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates (1995) J Appl Cryst, 28, pp. 768-773 Gralle, M., Botelho, M.M., Oliveira, C.L.P., Torriani, I., Ferreira, S.T., Solution studies and structural model of the extracellular domain of human amyloid precursor protein (2002) Biophys J, 83, pp. 3513-3524 Borges, J.C., Hannes, F., Craievich, A.F., Hansen, L.D., Ramos, C.H.I., Free human mitochondrial GrpE is a symmetric dimer in solution (2003) J Biol Chem, 278, pp. 35337-35344 Chou, W.C., Liao, K.W., Lo, Y.C., Jiang, S.Y., Yeh, M.Y., Roffler, S.R., Expression of chimeric monomer and dimer proteins on the plasma membrane of mammalian cells (1999) Biotechnol Bioeng, 65, pp. 160-169 Meyer, R.D., Rahimi, N., Comparative structure-function analysis of VEGFR-1 and VEGFR-2: What have we learned from chimeric systems? (2003) Ann NY Acad Sci, 995, pp. 200-207 Rizzuto, R., Brini, M., Pizzo, P., Murgia, M., Pozzan, T., Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells (1995) Curr Biol, 5, pp. 635-642 Shin, S.U., Morrison, S.L., Production and properties of chimeric antibody molecules (1989) Methods Enzymol, 178, pp. 459-476 Chamberlin, S.G., Brennan, L., Puddicombe, S.M., Davies, D.E., Turner, D.L., Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor (2001) Eur J Biochem, 268, pp. 6247-6255 Dey, B., Del Castillo, C.S., Berger, E.A., Neutralization of human immunodeficiency virus type 1 by sCD4-17b, a single-chain chimeric protein, based on sequential interaction of gp120 with CD4 and coreceptor (2003) J Virol, 77, pp. 2859-2865 Fontana, A., Fassina, G., Vita, C., Dalzoppo, D., Zamai, M., Zambonin, M., Correlation between sites of limited proteolysis and segmental mobility in thermolysin (1986) Biochemistry, 25, pp. 1847-1851 Li, Z., Gergely, J., Tao, T., Proximity relationships between residue 117 of rabbit skeletal troponin-I and residues in troponin-C and actin (2001) Biophys J, 81, pp. 321-333 Oliveira, D.C., Reinach, F.C., The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I (2003) Eur J Biochem, 270, pp. 2937-2944 Lakowicz, J.R., Gryczynski, I., Cheung, H.C., Wang, C.K., Johnson, M.L., Joshi, N., Distance distributions in proteins recovered by using frequency-domain fluorometry. Applications to troponin I and its complex with troponin C (1988) Biochemistry, 27, pp. 9149-9160 Heinohen, J.K., Lahti, R.J., A new and convenient calorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase (1987) Anal Biochem, 113, pp. 313-317 Oliveira, C.L.P., TRATID - Computer program for SAXS data treatment (2003) LNLS Technical Manual MT 01/2003 Semenyuk, V., Svergun, D.I., GNOM - A program package for small-angle scattering data processing (1991) J Appl Crystal, 24, pp. 537-540 Svergun, D.I., Petoukhov, M.V., Koch, M.H.J., Determination of domain structure of proteins from X-ray solution scattering (2001) Biophys J, 80, pp. 2946-2953 Petoukhov, M.V., Eady, N.A.J., Brown, K.A., Svergun, D.I., Addition of missing loops and domains to protein models using X-ray solution scattering (2002) Biophys J, 83, pp. 3113-3125 De La Torre, J.C., Huertas, M.L., Carrasco, B., Calculation of hydrodynamic properties of globular proteins from their atomic-level structure (2000) Biophys J, 78, pp. 719-730 Botelho, M.G., Gralle, M., Oliveira, C.L.P., Torriani, I.L., Ferreira, S.T., Folding and stability of the extracellular domain of the human amyloid precursor protein (2003) J Biol Chem, 278, pp. 34259-34267 Svergun, D.I., Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing (1999) Biophys J, 76, pp. 2879-2886 Svergun, D.I., Petoukhov, M.V., (2003) DAMAVER - Set of Programs to Align the Models Provided by DAMMIN and GASBOR and to Build 'the Most Probable' Model - Beta Version, , http://www.embl-hamburg.de/ExternalInfo/Research/Sax/damaver.html Kozin, M.B., Svergun, D.I., Automated matching of high- and low-resolution structural models (2001) J Appl Cryst, 34, pp. 33-41