Sequence and expression of amphioxus alkali myosin light chain (AmphiMLC-alk) throughout development: Implications for vertebrate myogenesis

Developmental Biology

Volumn 171, Issue 2, 1995, Pages 665-676

  Holland, Linda Z ^a   Pace, Douglas A ^b   Blink, Meriko L ^c   Kene, Mamata ^b   Holland, Nicholas D ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BRANCHIOSTOMA LANCEOLATUM; VERTEBRATA;

EID: 0028971378     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1006/dbio.1995.1313     Document Type: Article

References (54)

1. Ainger, K., Avossa, D., Morgan, F., Hill, S.J., Barry, C., Barbarese, E., and Carson, J. H. (1993), Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes. J. Cell Biol. 123, 431-441.
2. Baba, M. L., Goodman, M., Berger-Cohn, J., Démaillé, J. G., and Matsuda, G. (1984). The early adapative evolution of calmodulin. Mol Biol. Evol, 1, 442-455.
3. Barker, W. C., Ketcham, L., and Dayhoff, M. O. (1978). The troponin C superfamily. In "Atlas of Protein Sequence and Structure," Vol. 5, pp. 273-284. National Biomedical Research Foundation, Silver Spring, MD.
4. Barouch, W. W., Breese, K. E., Davidoff, S. A., Leszlyk, J., Szent-Gyorgyi, A. G., Theibert, J. L., and Collins, J. H. (1991). Amino acid sequence of myosin essential and regulatory light chains from two clam species: Comparison with other molluscan myosin light chains. J. Muse. Res. Cell. Motil. 12, 321-332.
5. Barton, P. J. R., and Buckingham, M. E. (1985). The myosin alkali light chain proteins and their genes. Biochem. J. 231, 249-261.
6. Barton, P. J. R., Cohen, I., Sassoon, D., Weydert, A., and Buckingham, M. E. (1988). Structure and sequences of the myosin alkali light chain gene expressed in adult cardiac atria and fetal striated muscle. J. Biol. Chem. 263, 12669-12676.
7. Benterbusch, R., Herverg, F. W., Melzer, W., and Thieleczek, R. (1992). Excitation-contraction coupling in a pre-vertebrate twitch muscle: The myotomes of Branchiostoma lanceolatum. J. Membr. Biol. 129, 237-252.
8. Chan, S. J., Cao, Q.-P., and Steiner, D. F. (1990). Evolution of the insulin superfamily: Cloning of a hybrid insulin/insulin-like growth factor cDNA from amphioxus. Proc. Natl. Acad. Sci. USA 87, 9319-9323.
9. Chomczynski, P., and Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
10. Collins, J. H. (1991). Myosin light chains and troponin C: Structural and evolutionary relationships revealed by amino acid sequence comparisons. J. Muse. Res. Cell Motil. 12, 3-25.
11. Crockford, T., and Johnston, I. A. (1993). Developmental changes in the composition of myofibrillar proteins in the swimming muscles of Atlantic herring, Clupea harengus. Mar. Biol. 115, 15-22.
12. Dalla Libera, L., Carpene, E., Thiebert, and Collins, J. H. (1991). Fish myosin alkali light chains originate from two different genes. J. Muse. Res. Cell Motil. 12, 366-371.
13. Falkenthal, S., Parker, V. P., Mattox, W. M., and Davidson, N. (1984). Drosophila melanogaster has only one myosin alkali light chain gene which encodes a protein with considerable amino acid sequence homology to chicken myosin alkali light chains. Mol Cell. Biol. 4, 956-965.
14. Feinberg, A. P., and Vogelstein, B. (1983). A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132, 6-13.
15. Flood, P. R. (1968). Structure of the segmental trunk muscles in amphioxus, with notes on the course and "endings" of the so-called ventral root fibers. Z. Zellforseh. Mikrosk. Anat. 132, 6-13.
16. Flood, P. R. (1975). Fine structure of the notochord of amphioxus. Symp. Zool. Soc. London 36, 81-104.
17. Fodor, W. L., Darras, B., Seharaseyon, J., Falkenthal, S., Francke, U., and Vanin, E. F. (1989). Human ventricular/slow twitch myosin alkali light chain gene characterization sequence, and chromosomal localization. J. Biol. Chem. 26, 2143-2149.
18. Fujisawa-Sehara, A., Nabeshima, Y., Kamiya, T., Uetsuki, T., Asakura, A., and Nabeshima, Y. (1992). Differential transactivation of muscle-specific regulatory elements including the myosin light chain box by chicken MyoD, myogenin and mrf4. J. Biol. Chem. 267, 31-38.
19. Garcia-Fernàndez, J., and Holland, P. W. H. (1994). Archetypal organization of the amphioxus Hox gene cluster. Nature 370, 563-566.
20. Goodwin, E. B., Szent-Gyorgi, A. G., and Leinwand, L. A. (1987). Cloning and characterization of the scallop essential and regulatory myosin light chain cDNAs. J. Biol. Chem. 262, 11052-11056.
21. Grieshammer, U., Sassoon, D., and Rosenthal, N. (1992). A transgene target for positional regulators marks early rostrocau-dai specification of myogenic lineages. Cell 69, 79-93.
22. Guthrie, D. M., and Banks, J. R. (1970). Observations on the electrical and mechanical properties of the myotomes of the lancelet (Branchiostoma lanceolatum). J. Exp. Biol. 52, 401-417.
23. Hailstones, D. L., and Gunning, P. W. (1990). Characterization of human myosin light chains Isa and 3nm: Implications for isoform evolution and function. Mol. Cell. Biol. 10, 1095-1104.
24. Holland, L. Z., Holland, P. W. H., and Holland, N. D. (1995). Revealing homologies between body parts of distantly related animals by in situ hybridization to developmental genes: Amphioxus vs vertebrates. In "Molecular Approaches to Zoology and Evolution" (S. Palumbi and J. D. Ferraris, Eds.), in press. Wiley, New York.
25. Holland, N. D., and Holland, L. Z. (1990). Fine structure of the mesothelia and extracellular materials in the coelomic fluid of the fin boxes, myocoels and sclerocoels of a lancelet, Branchiostoma floridae. Acta Zool. (Stockholm) 71, 225-234.
26. Holland, N. D., and Holland, L. Z. (1993). Embryos and larvae of invertebrate deuterostomes. In "Essential Developmental Biology: A Practical Approach" (C. D. Stem and P. W. H. Holland, Eds.), pp. 21-32. IRL Press, Oxford.
27. Holland, P. W. H. (1992). Homeobox genes in vertebrate evolution. BioEssays 14, 267-273.
28. Holland, P. W. H. (1993). Cloning genes using the polymerase chain reaction. In "Essential Developmental Biology: A Practical Approach" (C. D. Stern and P. W. H. Holland, Eds.), pp. 243-256. IRL Press, Oxford.
29. Holland, P. W. H., Holland, L. Z., Williams, N. A., and Holland, N. D. (1992). An amphioxus homeobox gene: Sequence conservation, spatial expression during development and insights into vertebrate evolution. Development 116, 653-661.
30. Holland, P. W. H., Garcia-Fernàndez, J., Holland, L. Z., Williams, N. A., and Holland, N. (1994a). The molecular control of spatial patterning in amphioxus. J. Marine Biol. Assoc. UK 74, 49-60.
31. Holland, P. W. H., Garciz-Fernàndez, J., Williams, N. A., and Sidow, A. (1994b). Gene duplications and the origins of vertebrate development. Development (suppl.) 125-133.
32. Holtzer, H., Marshall, J. M., and Finck, H. (1957). An analysis of myogenesis by the use of fluorescent antimyosin. J. Biophys. Biochem. Cytol. 3, 705-723.
33. Johnston, I. A., and Home, Z. (1994). Immunocytochemical investigations of muscle differentiation in the Atlantic herring (Clupea harengus: Teleostei). J. Mai. Biol. Assoc. UK 74, 79-91.
34. Kislauskis, E. H., Li, Z., Singer, R. H., and Taneja, K. L. (1993). Isoform-specific 3'-untranslated sequences sort α-cardiac and β-cytoplasmic actin messenger RNAs to different cytoplasmic compartments. J. Cell Biol. 123, 165-172.
35. Kwon, H., Goodwin, E. B., Nyitray, L., Berliner, E., O’Neall-Hennessey, E., Melandri, F. D., and Szent-Gyorgyi, A. G. (1990). Isolation of the regulatory domain of scallop myosin: Role of the essential light chain in calcium binding. Proc. Natl. Acad. Sci. USA 87, 4771-4775.
36. Lash, J. A., Helper, D.J., Klug, M., Nicolozakes, A. W., and Hathaway, D. R. (1990). Nucleotide and deduced amino acid sequence of cDNAs encoding 2 isoforms for the 17, 000 Dalton myosin light chain in bovine aortic smooth muscle. Nucleic Acids Res. 18, 71-76.
37. Lehman, W., and Szent-Gyorgi, A. G. (1975). Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom. J. Gen. Physiol. 66, 1-30.
38. Lyons, G. E., Ontell, M., Cox, R., Sassoon, D., and Buckingham, M. (1990). The expression oi myosin genes in developing skeletal muscle in the mouse embryo. J. Cell Biol. 111, 197-223.
39. Nabeshima, Y., Fujikura, Y., Muramatsu, M., and Ogata, K. (1982). Molecular cloning and nucleotide sequences of the complementary DNAs to chicken skeletal muscle myosin 2 alkali light chain messenger RNAs. Nucleic Acids Res. 10, 6099-6110.
40. Nabeshima, Y., Nabashima, Y.-I., Nonomura, Y., and Fujii-Kuriyama, Y. (1987). Non-muscle and smooth muscle myosin light chain messenger RNA are generated from a single gene by tissue-specific alternative RNA splicing. J. Biol. Chem. 262, 10608-10612.
41. Nabeshima, Y., Kawashima, M., Nakamura, S., Nonomura, Y., and Fujikura, Y. (1988). Isolation of the chick myosin alkali light chain gene expressed in embryonic gizzard muscle and transitional expression of the light chain gene family in vivo. J. Mol. Biol. 204, 497-505.
42. Pomeroy, M. E., Lawrence, J. B., Singer, R. H., and Billings-Gagliardi, S. (1991). Distribution of myosin heavy chain mRNA in embryonic muscle tissue visualized by ultrastructural in situ hybridization. Dev. Biol. 143, 58-67.
43. Rosenthal, N., Berglund, E. B., Wentworth, B. M., Donoghue, M., Winter, B., Bober, E., Braun, T., and Arnold, H.-H. (1990). A highly conserved enhancer downstream of the human MLC1/3 locus is a target for multiple myogenic determination factors. Nucleic Acids Res. 18, 6239-6246.
44. Rotter, N., Zimmerman, K., Poustka, A., Soussi-Yanicostas, N., and Starzinski-Powitz, A. (1991). The human embryonic myosin alkali light chain gene: Use of alternative promoters and 3' non-coding regions. Nucleic Acids Res. 19, 14497-14504.
45. Russell, B., and Dix, D. J. (1992). Mechanisms tot intracellular distribution of mRNA: In situ hybridization studies in muscle. Am. J. Physiol. 262, C1-C8.
46. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989). "Molecular Cloning: A Laboratory Manual," 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
47. Seidel, U., and Arnold, H. H. (1989). Identification of the functional promoter regions in the human gene encoding the myosin alkali light chains MLC1 and MLC3 of fast skeletal muscle. J. Biol. Chem. 264, 6109-6117.
48. Takagi, T., and Konishi, K. (1983). Amino acid sequence of Troponin C obtained from ascidian [Halocynthia roietzi) body wall muscle. J. Biochem. 94, 1753-1760.
49. Takagi, T., Kudoh, S., and Konishi, K. (1986). The amino acid sequence of ascidian (Halocynthia loietzi) myosin light chains. Biochim. Biophys. Acta 874, 318-325.
50. Takagi, T., Petrova, T., Comte, M., Kuster, T., Heizmann, C. W., and Cox, J. A. (1994). Characterization and primary structure of amphioxus troponin C. Eur. J. Biochem. 221, 537-546.
51. Takano-Ohmuro, H., Obinata, T., Kawashima, M., Masaki, T., and Tanaka, T. (1985). Embryonic chicken skeletal, cardiac, and smooth muscles express a common embryo-specific myosin light chain. J. Cell Biol. 100, 2025-2030.
52. Uetsuki, T., Nabeshima, Y., Fujisawa-Sehara, A., and Nabeshima, Y.-I. (1990). Regulation of the chicken embryonic myosin light-chain (L23) gene: Existence of a common regulatory element shared by myosin alkali light-chain genes. Mol. Cell. Biol. 10, 2562-2569.
53. Youn, B. W., and Malacinski, G. M. (1981). Comparative analysis of amphibian somite morphogenesis: Cell rearrangement patterns during rosette formation and myoblast fusion. J. Embryol. Exp. Morphol. 66, 1-26.
54. Welsch, U. (1968). Beobachtungen fiber die Feinstruktur der Haut und des äusseren Atrialepitheln von Branchiostoma lanceolatum Pall. Z. Zellforsch. Mikrosk. Anat. 88, 565-575.