Role of the head-to-tail overlap region in smooth and skeletal muscle β-tropomyosin

Biochemistry

Volumn 47, Issue 1, 2008, Pages 388-397

  Coulton, Arthur T ^a   Koka, Kezia ^a   Lehrer, Sherwin S ^b   Geeves, Michael A ^a  

^a UNIVERSITY OF KENT   (United Kingdom)

^b BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; NON-MUSCLE CELLS; TROPOMYOSIN;

ACETYLATION; AMINO ACIDS; CELLS; MUSCLE;

PROTEINS;

ACTIN; AMINO ACID; BETA TROPOMYOSIN; MUTANT PROTEIN; RECOMBINANT PROTEIN; TROPOMYOSIN; TROPONIN T; UNCLASSIFIED DRUG;

ACTIN FILAMENT; ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; EXON; HUMAN; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SKELETAL MUSCLE; SMOOTH MUSCLE;

ACTINS; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CHICKENS; FLUORESCENCE; HUMANS; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; MUSCLE, SMOOTH; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN ISOFORMS; RABBITS; SEQUENCE HOMOLOGY, AMINO ACID; TROPOMYOSIN;

EID: 37849009368     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701144g     Document Type: Article

References (52)

1. Smillie, L. B. (1979) Stmcture and functions of tropomyosins from muscle and non-muscle sources, Trends Biochem. Sci. 4, 151-154.
2. Lees-Miller, J. P., and Helfman, D. M. (1991) The molecular basis for tropomyosin diversity, BioEssays 13, 429-437.
3. Perry, S. V. (2001) Vertebrate tropomyosin: Distribution, properties and function, J. Muscle Res. Cell Motil. 22, 5-49.
4. Ruiz-Opazo, N., and Nadal-Ginard, B. (1987) Alpha tropomyosin gene organisation. Alternative splicing of duplicated isotype-specific exons accounts for the production of smooth and striated muscle isoforms, J. Biol. Chem. 262, 4755-4765.
5. Lees-Miller, J. P., Goodwin, L. O., and Helfman, D. M. (1990) Three novel brain isoforms are expressed from the rat α-tropomyosin gene through the use of alternative promoters and alternative RNA processing, Mol. Cell. Biol. 10, 1729-1742.
6. Wieczorek, D. F., Smith, C. W. J., and Nadal-Ginard, B. (1988) The rat α-tropomyosin gene generates a minimum of six different mRNA's coding for striated, smooth, and non-muscle isoforms by alternative splicing, Mol. Cell. Biol. 8, 679-694.
7. Basi, G. S., and Storti, R. V. (1986) Structure and DNA sequence of the Tm1 gene from Drosophila melanogaster. J. Biol. Chem. 261, 817-827.
8. Heald, R. W., and Hitchcock-Degregori, S. E. (1988) The structure of the amino terminus of tropomyosin is critical for binding to actin in the absence and presence of troponin, J. Biol. Chem. 263, 5254-5259.
9. Palm, T., Greenfield, N. J., and Hitchcock-Degregori, S. E. (2003) Tropomyosin ends determine the stability and functionality of overlap and troponin T complexes, Biophys. J. 84, 3181-3189.
10. Kluwe, L., Maeda, K., Miegel, A., Fujita-Becker, S., Maeda, Y., Talbo, G., Houthaeve, T., and Kellner, R. (1995) Rabbit skeletal muscle αα-tropomyosin expressed in baculovirus-infected insect cells possesses the authentic N-terminus structure and functions, J. Muscle Res. Cell Motil. 16, 103-110.
11. Monteiro, P. B., Lataro, R. C., Ferro, J. A., and Reinach, F d. C. (1994) Functional α-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group, J. Biol. Chem. 269, 10461-10466.
12. Coulton, A., Lehrer, S. S., and Geeves, M. A. (2006) Functional homodimers and heterodimers of recombinant smooth mucle tropomyosin, Biochemistry 45, 12853-12858.
13. Eisenberg, E., and Kielley, W. W. (1974) Troponin-tropomyosin complex. Column chromatographic separation and activity of the three active troponin components with and without tropomyosin present, J. Biol. Chem. 249, 4742-4748.
14. Lehrer, S. S. (1975) Intramolecular crosslinking of tropomyosin via disulfide bond formation: Evidence for chain register, Proc. Natl. Acad. Sci. U.S.A. 72, 3377-3381.
15. Bronson, D. D., and Schachat, F. H. (1982) Heterogeneity of contractile proteins. Differences in tropomyosin in fast, mixed, and slow skeletal muscles of the rabbit, J. Biol. Chem. 257, 3937-3944.
16. Sanders, C., Burtnik, L. D., and Smillie, L. B. (1986) Native chicken gizzard tropomyosin is predominantly a βγ-heterodimer, J. Biol. Chem. 261, 12774-12778.
17. Jancso, A., and Graceffa, P. (1990) Smooth muscle tropomyosin coiled-coil dimers. Subunit composition, assembly and end-to-end interaction, J. Biol. Chem. 266, 5891-5897
18. Lehrer, S. S., and Stafford, W. F. (1991) Preferential assembly of the tropomyosin heterodimer: Equilibrium studies, Biochemistry 30, 5682-5688.
19. Cho, Y. J., and Hitchcock-Degregori, S. E. (1991) Relationship between alternatively spliced exons and functional domains in tropomyosin, Proc. Natl. Acad. Sci. U.S.A. 88, 10153-10157.
20. Hammell, R. L., and Hitchcock-Degregori, S. E. (1996) Mapping the functional domains within the carboxyl terminus of α-tropomyosin encoded by the alternatively spliced ninth exon, J. Biol. Chem. 271, 4236-4242.
21. Lehrer, S. S., Golitsina, N. L., and Geeves, M. A. (1997) Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity. The role of tropomyosin flexibility and end-to-end interactions, Biochemistry 36, 13449-13454.
22. Moraczewska, J., and Hitchcock-Degregori, S. E. (2000) Independent functions for the N- and C-termini in the overlap region of tropomyosin, Biochemistry 39, 6891-6897.
23. McLachlan, A. D., and Stewart, M. (1975) Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure, J. Mol. Biol. 98, 293-304.
24. Ooi, T., Mihashi, K., and Kobayashi, H. (1962) On polymerisation of tropomyosin, Arch. Biochem. Biophys. 98, 1-11.
25. Sousa, A. D., and Farah, C. S. (2002) Quantitative analysis of tropomyosin linear polymerization equilibrium as a function of ionic strength, J. Biol. Chem. 277, 2081-2088.
26. Johnson, P., and Smilie, L. B. (1977) Polymerisability of rabbit skeletal tropomyosin: Effects of enzymic and chemical modifications, Biochemistry 16, 2264-2269.
27. Hitchcock-Degregori, S. E., and Heald, R. W. (1987) Altered actin and troponin binding of amino-terminal variants of chicken striated muscle α-tropomyosin expressed in Escherichia coli, J. Biol. Chem. 262, 9730-9735.
28. Phillips, G. N., Jr., Fillers, J. P., and Cohen, C. (1986) Tropomyosin crystal structure and regulation, J. Mol. Biol. 192, 111-131.
29. Whitby, F. G., and Phillips, G. N., Jr. (2000) Crystal structure of tropomyosin at 7 Å resolution, Proteins 38, 49-59.
30. Greenfield, N. J., Huang, Y. J., Swapna, G. V. T., Bhattacharya, A., Rapp, B., Singh, A., Montelione, G. T., and Hitchcock-Degregori, S. E. (2006) Solution NMR structure of the junction between tropomyosin molecules: Implications for actin binding and regulation, J. Mol. Biol. 364, 80-96.
31. Greenfield, N. J., Swapna, G. V., Huang, Y., Palm, T., Grabowski, S., Montelione, G. T., and Hitchcock-Degregori, S. E. (2003) The structure of the carboxyl terminus of striated α-tropomyosin in solution reveals an unusual parallel arrangement of interacting α-helices, Biochemistry 42, 614-619.
32. Bacchiochi, C., Graceffa, P., and Lehrer, S. S. (2004) Myosin induced movement of αα, αβ, and ββ smooth muscle tropomyosin on actin observed by multisite FRET, Biophys. J. 86, 2295-2307.
33. Kluwe, L., Maeda, K., Miegel, A., Fujita-Becker, S., Maeda, Y., Talbo, G., Houthaeve, T., and Kellner, R. (1995) Rabbit skeletal muscle αα-tropomyosin expressed in baculovirus-infected inect cells possesses the authentic N-terminus structure and functions, J. Muscle Res. Cell Motil. 16, 103-110.
34. Clos, J., and Brandau, S. (1994) pJC20 and pJC40: Two high-copy-number vectors for T7 RNA polymerase dependant expression of recombinant genes in Eschericia coli, Protein Expression Purif. 5, 133-137.
35. Kremneva, E., Nikolaeva, O., Maytum, R., Arutyunyan, A. M., Kleimenov, S. Y., Geeves, M. A., and Levitsky, D. I. (2006) Thermal unfolding of smooth muscle and nonmuscle tropomyosin α-homodimers with alternatively spliced exons, FEBS J. 273, 588-600.
36. Maytum, R., Lehrer, S. S., and Geeves, M. A. (1999) Cooperativity and switching within the three-state model of muscle regulation, Biochemistry 38, 1102-1110.
37. Potter, J. D. (1982) Preparation of troponin and its subunits, Methods Enzymol. 85 (Part B), 241-263.
38. 2- and COOH-terminal domains of troponin T. ATPase activation and binding to troponin I and troponin C, J. Biol. Chem. 273, 10594-10601.
39. Weeds, A. G., and Taylor, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin, Nature 257, 54-56.
40. Spudich, J. A., and Watt, S. (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin, J. Biol. Chem. 246, 4866-4871.
41. Cooper, J. A. (1987) Effects of cytochalasin and phalloidin on actin, J. Cell Biol. 105, 1473-1478.
42. McKillop, D. F., and Geeves, M. A. (1993) Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament, Biophys. J. 65, 693-701.
43. Vibert, P., Craig, R., and Lehman, W. (1997) Steric model for activation of muscle thin filaments, J. Mol. Biol. 266, 8-14.
44. Golitsina, N. L., and Lehrer, S. S. (1999) Smooth muscle α-tropomyosin crosslinks to caldesmon, to actin and to myosin subfragment 1 on the muscle thin filament, FEBS Lett. 463, 146-150.
45. Graceffa, P. (1989) In register homodimers of smooth muscle tropomyosin, Biochemistry 28, 1282-1287.
46. Paulucci, A. A., Katsuyama, A. M., Sousa, A. D., and Farah, C. S. (2004) A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerisation, Eur. J. Biochem. 271, 589-600.
47. Brown, J. H., Kim, K. H., Jun, G., Greenfield, N. J., Dominguez, R., Volkmann, N., Hitchcock-Degregori, S. E., and Cohen, C. (2001) Deciphering the design of the tropomyosin molecule, Proc. Natl. Acad. Sci. U.S.A. 98, 8496-8501.
48. Cassell, M., and Tobacman, L. S. (1996) Opposite effects of myosin subfragment 1 on binding of cardiac troponin and tropomyosin to the thin filament, J. Biol. Chem. 271, 12867-12872.
49. Wegner, A. (1979) Equilibrium of the actin-tropomyosin interaction, J. Mol. Biol. 311, 1027-1036.
50. Cho, Y. J. (2000) The carboxyl terminal amino acid residues glutamine276-threonine277 are important for actin affinity of the unacetylated smooth α-tropomyosin, J. Biochem. Mol. Biol. 33, 531-536.
51. Boussouff, S. E., Maytum, R., Jaquet, K., and Geeves, M. A. (2007) Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments, J. Muscle Res. Cell Motil. 28, 49-58.
52. Maytum, R., Konrad, M., Lehrer, S. S., and Geeves, M. A. (2001) Regulatory properties of tropomyosin effects of length, isoform, and N-terminal sequence, Biochemistry 40, 7334-7441.