Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity

Structure

Volumn 4, Issue 3, 1996, Pages 323-337

  Improta, Sabina ^a   Politou, Anastasia S ^a   Pastore, Annalisa ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Connectin; Elasticity; Immunoglobulin superfamily; Muscle; NMR

Indexed keywords

CONNECTIN; IMMUNOGLOBULIN; MUSCLE PROTEIN; PROTEIN KINASE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; IMMUNOGLOBULINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUSCLE PROTEINS; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

EID: 0030584660     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00036-6     Document Type: Article

References (69)

1. Labeit, S. et al., & Trinick, J. (1990). A regular pattern of two types of 100-residue motif in the sequence of titin. Nature 345, 273-276.
2. Labeit, S. & Kolmerer, B. (1995). Titins, giant proteins in charge of muscle ultrastructure and elasticity. Science 270, 293-296.
3. Nave, R., Fuerst, D.O. & Weber, K. (1989). Visualization of the polarity of isolated titin molecule: a single globular head on a long thin rod as the M-band anchoring domain? J. Cell. Biol. 109, 2177-2187.
4. Fuerst, D.O., Osborn, M., Nave, R. & Weber, K. (1988). The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M-line. J. Cell Biol. 106, 1563-1572.
5. Maruyama, K. (1994). Connectin, an elastic protein of striated muscle. Biophys. Chem. 50, 73-85.
6. Trinick, J. (1994). Titin and nebulin: protein rulers in muscle? Trends Biochem. Sci. 19, 405-408.
7. Keller, T.C.S. (1995). Structure and function of titin and nebulin. Curr. Opin. Cell Biol. 7, 32-38.
8. Soteriou, A., Gamage, M. & Trinick, J. (1993). A survey of interactions made by the giant protein titin. J. Cell Sci. 104, 119-123.
9. Funatsu, T. et al., & Tsukita, S. (1993). Elastic filaments in situ in cardiac muscles: deep-etch replica analysis in combination with selective removal of actin and myosin filaments. J. Cell Biol. 120, 711-724.
10. Horowits, R., Maruyama, K. & Podolsky, R.J. (1989). Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle. J. Cell Biol. 109, 2169-2176.
11. Vinkemeier, U., Obermann, W., Weber, K. & Fuerst, D.O. (1993). The globular head domain of titin extends into the center of the sarcomeric M band. cDNA cloning, epitope mapping and immunoelectron microscopy of two titin-associated proteins. J. Cell Sci. 106, 319-330.
12. Gautel, M., Leonard, K. & Labeit, S. (1993). Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts. EMBO J. 10, 3827-3834.
13. Pfuhl, M. & Pastore, A. (1995). Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: a new member of the I-set. Structure 3, 391-401.
14. Harpaz, Y. & Chothia, C. (1994). Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238, 528-539.
15. Maruyama, K., et al., & Maruyama, K. (1993). A novel domain sequence of connectin localized at the I-band of skeletal muscle sarcomeres: homology to neurofilament subunits. Biochem. Biophys. Res. Commun. 194, 1288-1291.
16. Sebestyen, M.G., Wolff, J.A. & Greaser, M.L. (1995). Characterization of a 5.4 kb cDNA fragment from the Z-line region of a rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases. J. Cell Sci. 108, 3029-3037.
17. Politou, A.S., Gautel, M., Pfuhl, M., Labeit, S. & Pastore, A. (1994). Immunoglobulin-type domains of titin: same fold, different stability? Biochemistry 33, 4730-4737.
18. Politou, A.S., Thomas, D.J. & Pastore, A. (1995). The folding and stability of titin immonoglobulin-like modules, with implications for the mechanism pf elasticity. Biophys. J. 69, 2601-2610.
19. Itoh, Y. et al., & Shimizu, T. (1988). Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. J. Biochem. 104, 504-508.
20. Trombitas, K., Baatsen, P.H.W.W., Kellermayer, M.S.Z. & Pollack, G.H (1991). Nature and origin of gap filaments in striated muscle. J. Cell Sci. 100, 809-814.
21. Wang, K., McCarter, R., Wright, J., Beverly, J. & Ramirez-Mitchell, R. (1991). Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension. Proc. Natl. Acad. Sci. USA 88, 7101-7105.
22. Soteriou, A., Clarke, A., Martin, S. & Trinick, J. (1993). Titin folding energy and elasticity. Proc. R. Soc. Lond. B Biol. Sci. 254, 83-86.
23. Erickson, H. P. (1994). Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. Proc. Natl. Acad. Sci. USA 91, 10114-10118.
24. Wang, K., McClure, J., Wright, J., Beverly, J. & Ramirez-Mitchell, R. (1993). Viscoelasticity of the sarcomere matrix of skeletal muscles: the titin-myosin composite filament is a dual-stage molecular spring. Biophys J. 64, 1167-1177.
25. Politou, A.S., Gautel, M., Joseph, C. & Pastore, A. (1994). Immunoglobulin-like domains of titin are stabilized by amino-terminal extension. FEBS Lett. 352, 27-31.
26. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids. John Wiley and Sons, NY.
27. Pastore, A. & Saudek, V. (1990). The relationship between chemical shifts and secondary structure in proteins. J. Magn. Reson. 90, 165-177.
28. Wishart, D.S., Sykes, B.D. & Richards, F.M. (1991). Relationship between nuclear magnetic resonance chemical shift and protein structure. J. Mol. Biol. 222, 331-333.
29. Chan, A.W.E., Hutchinson, E.G., Harris, D. & Thornton, J.M. (1993). Identification, classification, and analysis of beta-bulges in proteins. Protein Sci. 2, 1574-1590.
30. Wilmot, C.M. & Thornton, J.M. (1990). β-Turns and their distortions: a proposed new nomenclature. Protein Eng. 3, 479-493.
31. Kabat, E.A., Wu, T.T., Perry, H.M., Gottesman, K.S. & Foeller, C. (1991). Sequences of Proteins of Immunological Interest (5th Edn). NIH, Bethesda, MD.
32. Holden, H.M., Ito, M., Hartshorn, D.J. & Rayment, I. (1992). X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 Å resolution. J. Mol. Biol. 227, 840-851.
33. Jones, E.Y., et al., & Stuart, D.I. (1995). Crystal structure of an integrin binding fragment of vascular cell adhesion molecule-1 at 1.8 Å resolution. Nature 373, 539-544.
34. Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
35. Politou, A.S., Gautel, M., Improta, S., Vangelista, L. & Pastore, A. (1996). The elastic I-band region of titin is assembled by weakly interacting Ig-like domains. J. Mol. Biol. 255, 604-616.
36. Wang, J., et al. & Harrison, S.C. (1990). Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature 348, 411-418.
37. 2-terminal domains. Science 260, 979-983.
38. Thomas, D.J. (1992). The entropic tension of protein loops. J. Mol. Biol. 216, 457-463.
39. Lesk, A.M. & Chothia, C. (1988). Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint. Nature 335, 188-190.
40. Bodian, D.L., Jones, E.Y., Harlos, K., Stuart, D.I. & Davis, S.J. (1994). Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure 2, 755-766.
41. Jones, E.Y., et al., & Stuart, D.I. (1992). Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2. Nature 360, 232-239.
42. Huber, A.H., Wang, Y.M., Bieber, A.J. & Bjorkman, P.J. (1994). Crystal structure of tandem type-III fibronectin domains from Drosophila neuroglian at 2.0 Å. Neuron 12, 717-731.
43. Studier, F.W., Rosenberg, A.H., Dunn, J.J. & Dubbendorf, J.W. (1990). Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
44. Studier, F.W. & Moffat, B.A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130.
45. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
46. 1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113, 967-974.
47. Piotto, M., Saudek V. & Sklenar V. (1992). Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
48. 15N HSQC experiments optimized to retain full sensitivity. J. Magn. Reson. A 102, 241-245.
49. Kadkhodaei, M., Hwang, T. & Shaka, A.J. (1993). A simple windowless mixing sequence to suppress cross relaxation in TOCSY experiments. J. Magn. Reson. A 105, 104-107.
50. 15N-labeled proteins. J. Magn. Reson. 86, 110-126.
51. Shaka, A.J, Barker, P.B. & Freeman, R. (1985). Computer-optimized decoupling scheme for wideband applications and low-level operation. J. Magn. Reson. 64, 547-552.
52. Neidig, P., et al. & Kalbitzer, H.R. (1995). AURELIA, a program for computer-aided analysis of multidimensional NMR spectra. J. Biomol. NMR 6, 255-270.
53. Pardi, A., Billeter, M. & Wüthrich, K. (1984). Calibration of the angular dependence of the amide proton-Cα proton coupling constant, 3JHNα, in a globular protein. J. Mol. Biol. 180, 741-751.
54. Guentert, P., Braun, W. & Wüthrich, K. (1991). Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217, 517-530.
55. Wüthrich, K. & Braun, W. (1983). Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear resonance. J. Mol. Biol. 169, 949-961.
56. Brünger, A.T. (1993). XPLOR: A System for X-ray Crystallography and NMR, Version 3.1. Yale University Press, New Haven, CT.
57. Nilges, M. (1995). Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities. J. Mol. Biol. 245, 645-660.
58. Levy, R.M., Bassolino, D.A., Kitchen, D.B. & Pardi, A. (1989). Solution structures of proteins from NMR data and modeling: alternative folds for neutrophil peptide 5. Biochemistry 28, 9361-9372.
59. Guentert, P. & Wuthrich, K. (1991). Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle costraints. J. Biomol. NMR 1, 447-456.
60. Nilges, M., Gronenborn, A.M., Brünger, A.T. & Clore, G.M. (1988). Determination of the three-dimensional structures of proteins by simulated annealing with interproton distance restraints: application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng. 2, 27-38.
61. Kharrat, A., Macias, M.J., Gibson, T.J., Nilges, M. & Pastore, A. (1995). Structure of the dsRNA binding domain of E.coli RNase III. EMBO J. 14, 3563-3571.
62. Diamond, R. (1992). On the multiple simultaneous superposition of molecular structures by rigid body transformation. Proteins 1, 1279-1283.
63. Vriend, G. & Sander, C. (1993). Quality control of protein models: directional atomic contact analysis. J. Appl. Cryst. 26, 47-60.
64. Sippl, M.J. (1993). Recognition of errors in three-dimensional structures of proteins. Proteins 17, 355-362.
65. Dayringer, H.E., Tramontano, A., Sprang, S. & Fletterick, R.J. (1986). INSIGHT: an interactive molecular graphics package. J. Mol. Graphics 4, 82-87.
66. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Cryst. 24, 251-259.
67. Thompson, J., Higgins, D.G. & Gibson, T.J. (1994). CLUSTALW: 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.
68. Vriend, G. (1990). WHAT IF: a molecular modeling and drug design program. J. Mol. Graphics 8, 52-55.
69. Rost, B. Sander, C. & Schneider, R. (1994). PHD - a mail server for protein secondary structure prediction. CABIOS 10, 53-60.