In situ orientations of protein domains: Troponin C in skeletal muscle fibers

Molecular Cell

Volumn 11, Issue 4, 2003, Pages 865-874

  Ferguson, Roisean E ^a,d   Sun, Yin Biao ^b   Mercier, Pascal ^c   Brack, Andrew S ^b   Sykes, Brian D ^c   Corrie, John E T ^a   Trentham, David R ^a   Irving, Malcolm ^b  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^b KING'S COLLEGE LONDON   (United Kingdom)

^c CANADIAN INSTITUTES OF HEALTH RESEARCH   (Canada)

^d ST JAMES S UNIVERSITY HOSPITAL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; RHODAMINE; TROPONIN C;

ACTIN FILAMENT; ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DNA HELIX; DNA PROBE; FLUORESCENCE; IN SITU HYBRIDIZATION; MACROMOLECULE; MEASUREMENT; MUSCLE CONTRACTION; NONHUMAN; ORIENTATION; POLARIZATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; SKELETAL MUSCLE; STRUCTURE ACTIVITY RELATION;

EID: 0037961726     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00096-0     Document Type: Article

References (46)

1. Bell M.G., Dale R.E., van der Heide U.A., Goldman Y.E. Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges. Biophys. J. 83:2002;1050-1073.
2. Chase P.B., Kushmerick M.J. Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers. Biophys. J. 53:1988;935-946.
3. Cone R.A. Rotational diffusion of rhodopsin in the visual receptor mechanism. Nat. New Biol. 236:1972;39-43.
4. Corrie J.E.T., Craik J.S., Munasinghe V.R.N. A homobifunctional rhodamine for labeling proteins with defined orientations of a fluorophore. Bioconjug. Chem. 9:1998;160-167.
5. Corrie J.E.T., Brandmeier B.D., Ferguson R.E., Trentham D.R., Kendrick-Jones J., Hopkins S.C., van der Heide U.A., Goldman Y.E., Sabido-David C., Dale R.E.et al. Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction. Nature. 400:1999;425-430.
6. Cox J.A., Comte M., Stein E.A. Calmodulin-free skeletal-muscle troponin C prepared in the absence of urea. Biochem. J. 195:1981;205-211.
7. Craig R., Lehman W. The ultrastructural basis of actin filament regulation. Results Probl. Cell Differ. 36:2002;149-169.
8. Dale R.E., Hopkins S.C., van der Heide U.A., Marszalek T., Irving M., Goldman Y.E. Model-independent analysis of the orientation of fluorescent probes with restricted mobility in muscle fibers. Biophys. J. 76:1999;1606-1618.
9. Ebashi S., Endo M., Otsuki I. Control of muscle contraction. Q. Rev. Biophys. 4:1969;351-384.
10. Farah C.S., Reinach F.C. The troponin complex and regulation of muscle contraction. FASEB J. 9:1995;755-767.
11. 2 and COOH-terminal regions of skeletal muscle troponin I. J. Biol. Chem. 269:1994;5230-5240.
12. Forkey J.N., Quinlan M.E., Goldman Y.E. Protein structural dynamics by single-molecule fluorescence polarization. Prog. Biophys. Mol. Biol. 74:2000;1-35.
13. Gagné S.M., Tsuda S., Li M.X., Chandra M., Smillie L.B., Sykes B.D. Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci. 3:1994;1961-1974.
14. Gagné 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. Nat. Struct. Biol. 2:1995;784-789.
15. Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
16. Golosinska K., Pearlstone J.R., Borgford T., Oikawa K., Kay C.M., Carpenter M.R., Smillie L.B. Determination of and corrections to sequences of turkey and chicken troponins-C. J. Biol. Chem. 266:1991;15797-15809.
17. Gordon A.M., Homsher E., Regnier M. Regulation of contraction in striated muscle. Physiol. Rev. 80:2000;853-924.
18. Grabarek Z., Tao T., Gergely J. Molecular mechanism of troponin C function. J. Muscle Res. Cell Motil. 13:1992;383-393.
19. Greaser M.L., Gergely J. Reconstitution of troponin activity from three protein components. J. Biol. Chem. 246:1971;4226-4233.
20. Hazelgrove J.C. X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle. Cold Spring Harb. Symp. Quant. Biol. 37:1973;341-352.
21. Heeley D.H., Golosinska K., Smillie L.B. 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. 262:1987;9971-9978.
22. Herzberg O., James M.N.G. Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature. 313:1985;653-659.
23. Herzberg O., James M.N.G. Refined crystal structure of troponin C from turkey skeletal muscle at 2 Å resolution. J. Mol. Biol. 203:1988;761-779.
24. Hopkins S.C., Sabido-David C., van der Heide U.A., Ferguson R.E., Brandmeier B.D., Dale R.E., Kendrick-Jones J., Corrie J.E.T., Trentham D.R., Irving M.et al. Orientation changes of the myosin light chain domain during filament sliding in active and rigor muscle. J. Mol. Biol. 318:2002;1275-1291.
25. 2+-switch in the calmodulin superfamily Structure. 5:1997;1695-1711.
26. Huxley H.E. Structural changes in the actin- and myosin-containing filaments during contraction. Cold Spring Harb. Symp. Quant. Biol. 37:1973;361-376.
27. 147-163 induces a structural opening in human cardiac troponin-C. Biochemistry. 38:1999;8289-8298.
28. Ling N., Shrimpton C., Sleep J., Kendrick-Jones J., Irving M. Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle. Biophys. J. 70:1996;1836-1846.
29. 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. J. Biol. Chem. 272:1997;28494-28500.
30. Mercier P., Spyracopoulos L., Sykes B.D. Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I. Biochemistry. 40:2001;10063-10077.
31. Mercier P., Ferguson R.E., Irving M., Corrie J.E.T., Trentham D.R., Sykes B.D. The NMR structure of a bifunctional rhodamine labeled troponin C in complex with the regulatory "switch" peptide from troponin I; implications for in situ fluorescence studies in muscle fibers. Biochemistry. 42:2003;4333-4348.
32. Moss R.L., Giulian G.G., Greaser M.L. The effects of partial extraction of TnC upon the tension-pCa relationship in rabbit skinned skeletal muscle fibers. J. Gen. Physiol. 86:1985;585-600.
33. 2+-induced switching of troponin and tropomyosin on actin filaments as revealed by electron cryo-microscopy. J. Mol. Biol. 308:2001;241-261.
34. Parry D.A.D., Squire J.M. Structural role of tropomyosin in muscle regulation. analysis of x-ray diffraction patterns from relaxed and contracting muscles J. Mol. Biol. 75:1973;33-55.
35. Pearlstone J.R., Smillie L.B. Troponin T fragments. physical properties and binding to troponin C Can. J. Biochem. 56:1978;521-527.
36. Sabido-David C., Brandmeier B., Craik J.S., Corrie J.E.T., Trentham D.R., Irving M. Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethylrhodamine. Biophys. J. 74:1998;3083-3092. a.
37. Sabido-David C., Hopkins S.C., Saraswat L.D., Lowey S., Goldman Y.E., Irving M. Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibers. J. Mol. Biol. 279:1998;387-402. b.
38. Sanger F., Nicklens S., Coulsen A.R. DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci. USA. 74:1977;5463-5467.
39. Satyshur K.A., Rao S.T., Pyzalska D., Drendel W., Greaser M., Sundaralingam M. Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-Å resolution. J. Biol. Chem. 263:1988;1628-1647.
40. Slupsky C.M., Sykes B.D. NMR solution structure of calcium-saturated skeletal muscle troponin C. Biochemistry. 34:1995;15953-15964.
41. Soman J., Tao T., Phillips G.N. Conformational variation of calcium-bound troponin C. Proteins. 37:1999;510-511.
42. Strynadka N.C.J., Cherney M., Sielecki A.R., Li M.X., Smillie L.B., James M.N.G. Structural details of a calcium-induced molecular switch. X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 Å resolution J. Mol. Biol. 273:1997;238-255.
43. Sundaralingam M., Bergstrom R., Strasburg G., Rao S.T., Roychowdhury P., Greaser M., Wang B.C. Molecular structure of troponin C from chicken skeletal muscle at 3 Å resolution. Science. 227:1985;945-948.
44. 2+-dependent regulation of muscle contraction. J. Mol. Biol. 271:1997;728-750.
45. van der Heide U.A., Hopkins S.C., Goldman Y.E. A maximum entropy analysis of protein orientations using fluorescence polarization data from multiple probes. Biophys. J. 78:2000;2138-2150.
46. Vassylyev D.G., Takeda S., Wakatsuki S., Maeda K., Maeda Y. Crystal structure of troponin C in complex with troponin I fragment at 2.3-Å resolution. Proc. Natl. Acad. Sci. USA. 95:1998;4847-4852.