Binding of Calcium Ions to an Avian Flight Muscle Troponin T

Biochemistry

Volumn 43, Issue 9, 2004, Pages 2645-2655

  Zhang, Zhiling ^a   Jin, Jian Ping ^b   Root, Douglas D ^a  

^a UNIVERSITY OF NORTH TEXAS   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CALCIUM; DIMERS; FLUORESCENCE; MUSCLE; RNA;

STOPPED-FLOW ANALYSIS; TROPONIN T (TNT);

BIOCHEMISTRY;

CALCIUM GREEN 5N; CALCIUM ION; DIMER; FLUORESCENT DYE; TERBIUM; TROPOMYOSIN; TROPONIN T; UNCLASSIFIED DRUG;

ALTERNATIVE RNA SPLICING; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CALCIUM BINDING; CALCULATION; CHICKEN; COMPLEX FORMATION; FLUORESCENCE; METAL BINDING; MUSCLE CONTRACTION; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; SKELETAL MUSCLE;

NON-PROGRAMMATIC;

AMINO ACID SEQUENCE; ANIMALS; BINDING, COMPETITIVE; CALCIUM; CALCIUM-BINDING PROTEINS; CATIONS, DIVALENT; CHICKENS; COMPUTER SIMULATION; FLIGHT, ANIMAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE FIBERS, FAST-TWITCH; PROTEIN BINDING; PROTEIN ISOFORMS; TERBIUM; TROPONIN T;

ANIMALIA; AVES; GALLUS GALLUS;

EID: 1542297704     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035067o     Document Type: Article

References (47)

1. Leavis, P. C., and Gergely, J. (1984) Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16, 235-305.
2. Tobacman, L. S. (1996) Thin filament-mediated regulation of cardiac contraction. Annu. Rev. Physiol. 58, 447-81.
3. Heller, W. T., Abusamhadneh, E., Finley, N., Rosevear, P. R., and Trewhella, J. (2002) The solution structure of a cardiac troponin C-troponin I-troponin T complex shows a somewhat compact troponin C interacting with an extended troponin I-troponin T component. Biochemistry 41, 15654-63.
4. Smillie, L. B., Golosinska, K., and Reinach, F. C. (1988) Sequences of complete cDNAs encoding four variants of chicken skeletal muscle troponin T. J. Biol. Chem. 263, 18816-20.
5. Breitbart, R. E., and Nadal-Ginard, B. (1986) Complete nucleotide sequence of the fast skeletal troponin T gene. Alternatively spliced exons exhibit unusual interspecies divergence. J. Mol. Biol. 188, 313-24.
6. Cooper, T. A., and Ordahl, C. P. (1985) A single cardiac troponin T gene generates embryonic and adult isoforms via developmentally regulated alternate splicing. J. Biol. Chem. 260, 11140-8.
7. Jin, J. P., and Lin, J. J. C. (1989) Isolation and characterization of cDNA clones encoding embryonic and adult isoforms of rat cardiac troponin T. J. Biol. Chem. 264, 14471-7.
8. Jin, J. P., Huang, Q. Q., Yeh, H. I., and Lin, J. J. C. (1992) Complete nucleotide sequence and structural organization of rat cardiac troponin T gene. A single gene generates embryonic and adult isoforms via developmentally regulated alternative splicing. J. Mol. Biol. 227, 1269-76.
9. 2-terminal variable region of avian fast skeletal muscle troponin T: functional divergence on the basis of tolerance to structural drifting. J. Mol. Evol. 52, 103-16.
10. Wilkinson, J. M., Moir, A. J. G., and Waterfield, M. D. (1984) The expression of multiple forms of troponin T in chicken fast-skeletal muscle may result from differential splicing of a single gene. Eur. J. Biochem. 143, 47-56.
11. Miyazaki, J., Jozaki, M., Nakatani, N., Watanabe, T., Saba, R., Nakada, K., Hirabayashi, T., and Yonemura, I. (1999) The structure of the avian fast skeletal muscle troponin T gene: seven novel tandem-arranged exons in the exon x region. J. Muscle Res. Cell Motil. 20, 655-60.
12. Wilkinson, J. M. (1978) The components of troponin from chicken fast skeletal muscle. Biochem. J. 169, 229-38.
13. 2-terminal hypervariable region in the tolerance to acidosis. J. Biol. Chem. 273, 27858-66.
14. Jin, J.-P., and Smillie, L. B. (1994) An unusual metal-binding cluster found exclusively in the avian breast muscle troponin T of Galliformes and Craciforms. FEBS Lett. 341, 135-40.
15. Ogut, O., and Jin, J.-P. (1996) Expression, Zinc-Affinity purification, and characterization of a novel metal-binding cluster in troponin T: metal-stabilized α-helical structure and effects of the NH2-terminal variable region on the conformation of intact troponin T and its association with tropomyosin. Biochemistry 35, 16581-90.
16. 2-Terminal Variable Region and Functional Effects. Biochemistry 37, 14519-28.
17. 2-terminal variable region. Biochemistry 39, 11702-13.
18. Tobacman, L. B. (1988) Structure-function studies of the amino-terminal region of bovine cardiac troponin T. J. Biol. Chem. 263, 2668-72.
19. Ogut, O., Granzier, H., and Jin, J.-P. (1999) Acidic and basic troponin T isoforms in mature fast-twitch skeletal muscle and effect on contractility. Am. J. Physiol.: Cell Physiol. 276, C1162-70.
20. Aitken, A., and Learmonth, M. P. (2002) Protein determination by UV absorption in The Protein Protocols Handbook (Walker, J. M., Ed.) 2nd ed., pp 3-6, Humana Press, New Jersey.
21. Smillie, L. B. (1982) Preparation and identification of α- and β-tropomyosins. Methods Enzymol. 85, 234-41.
22. Luo, Y., Wu, J.-L., Li, B., Langsetmo, K., Gergely, J., and Tao, T. (2000) Photo-cross-linking of benzophenone-labeled single cysteine troponin I mutants to other thin filament proteins. J. Mol. Biol. 296, 899-910.
23. 2-terminal half and complete sequence. J. Biol. Chem. 253, 1137-48.
24. Naraghi, M. (1997) T-jump study of calcium binding kinetics of calcium chelators. Cell Calcium 22, 255-68.
25. Felts, A. K., Gallicchio, E., Wallqvist, A., and Levy, R. M. (2002) Distinguishing native conformations of proteins from decoys with an effective free energy estimator based on the OPLS all-atom force field and the surface generalized Born solvent model. Proteins 48, 404-22.
26. Liu, Y., and Beveridge, D. L. (2002) Exploratory studies of ab initio protein structure prediction: Multiple copy simulated annealing, AMBER energy functions, and a generalized Born/solvent accessibility solvation model. Proteins 46, 128-46.
27. Christensen, I. T., and Jorgensen, F. S. (1997) Molecular mechanics calculations of proteins. Comparison of different energy minimization strategies. J. Biomol. Struct. Dyn. 15, 473-88.
28. Sale, K., Sár, C., Sharp, T. A., Hideg, K., and Fajer, P. G. (2002) Structural determination of spin label immobilization and orientation: A Monte Carlo minimization approach. J. Magn. Reson. 156, 104-12.
29. Huang, E. S., Ram Samudrala, R., and Ponder, J. W. (1999) Ab initio fold prediction of small helical proteins using distance geometry and knowledge-based scoring functions. J. Mol. Biol. 290, 267-81.
30. Heeley, D. H., Golosinska, K., and Smillie, L. B. (1987) The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C. J. Biol. Chem. 262, 9971-8.
31. Brittain, H. G., Richardson, F. S., and Martin, R. B. (1976) Terbium (III) emission as a probe of calcium (II) binding sites in proteins. J. Am. Chem. Soc. 98, 8255-60.
32. Martin, R. B., and Richardson, F. S. (1979) Lanthanides as probes for calcium in biological systems. Q. Rev. Biophys. 12, 181-209.
33. Kilhoffer, M.-C., Demaille, J. G., and Gerard, D. (1980) Terbium as luminescent probe of calmodulin calcium-binding sites: Domains I and II contain the high-affinity sites. FEBS Lett. 116, 269-72.
34. Ortiz, A. R., Kolinski, A., and Skolnick, J. (1998) Nativelike topology assembly of small proteins using predicted restraints in Monte Carlo folding simulations. Proc. Natl. Acad. Sci. U.S.A. 95, 1020-5.
35. Gibbs, N., Clarke, A. R., and Sessions, R. B. (2001) Ab initio protein structure prediction using physicochemical potentials and a simplified off-lattice model. Proteins 43, 186-202.
36. Ishikawa, K., Yue, K., and Dill, K. A. (1999) Predicting the structures of 18 peptides using Geocore. Protein Sci. 8, 716-21.
37. Jones-Hertzog, D. K., and Jorgensen, W. L. (1997) Binding affinities for sulfonamide inhibitors with human thrombin using Monte Carlo simulations with a linear response method. J. Med. Chem. 40, 1539-49.
38. Åqvist, J., Medina, C., and Samuelsson, J. E. (1994) A new method for predicting binding affinity in computer-aided drug design. Protein Eng. 7, 385-91.
39. Sham, Y. Y., Chu, Z. T., Tao, H., and Warshel, A. (2000) Examining methods for calculations of binding free energies: LRA, LIE, PDLD-LRA, and PDLD/S-LRA: Calculations of ligands binding to an HIV protease. Proteins 39, 393-407.
40. 2+ regulation of muscle contraction. Biochemistry 13, 2697-703.
41. Johnson, J. D., Jiang, Y., and Rall, J. A. (1999) Intracellular EDTA mimics parvalbumin in the promotion of skeletal muscle relaxation. Biophys. J. 76, 1514-22.
42. Blum, H. E., Lehky, P., Kohler, L., Stein, E. A., and Fischer, E. H. (1977) Comparative properties of vertebrate parvalbumins. J. Biol. Chem. 252, 2834-8.
43. Cates, S. M., Berry, M. B., Ho, E. L., Li, Q., Potter, J. D., and Phillips, G. N., Jr. (1999) Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin. Structure 7, 1269-78.
44. Müntener, M., Käser, L., Weber, J., and Berchtold, M. W. (1995) Increase of skeletal muscle relaxation speed by direct injection of parvalbumin cDNA. Proc. Natl. Acad. Sci. U.S.A. 92, 6504-8.
45. Resetar, A. M., Stephens, J. M., and Chalovich, J. M. (2002) Troponin-tropomyosin: an allosteric switch or a steric blocker? Biophys. J. 83, 1039-49.
46. Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-50.
47. Merritt, E. A., and Bacon, D. J. (1997) Raster3D photorealistic molecular graphics. Methods Enzymol. 277, 505-24.