Dictyostelium discoideum Myosin: Isolation and Characterization of cDNAs Encoding the Regulatory Light Chain

LITERATURE CITED

• Adelstein, R. S., and M. A. Conti. 1975. Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity. Nature (London) 256:597–598.
   PubMed Web of Science ®Google Scholar
• Albrecht-Buehler, G.. 1976. The function of filipodia in spreading 3T3 mouse fibroblasts, p. 247–264. In R. Goldman, T. Pollard, and J. Rosenbaum (ed.). Cell motility. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Allison, A. C.. 1976. The role of contractile systems in endocytosis and exocytosis, p. 333–347. In S. V. Perry, A. Margreth, and R. S. Adelstein (ed.), Contractile systems of non-muscle tissues. North-Holland Publishing Co., Amsterdam.
   Google Scholar
• Berlot, C. H., P. N. Devreotes, and J. A. Spudich. 1987. Chemoattractant-elicited increases in Dictyostelium myosin phosphorylation are due to changes in myosin localization and increases in kinase activity. J. Biol. Chem. 262:3918–3926.
   PubMedGoogle Scholar
• Bourguignon, L. Y. W., M. L. Nagpal, and Y.-C. Hsing. 1981. Phosphorylation of myosin light chains during capping of mouse T-lymphoma cells. J. Cell Biol. 91:889–894.
   PubMedGoogle Scholar
• Carboni, J. M., and J. S. Condeelis. 1985. Ligand-induced changes in the location of actin, myosin. 95k protein, and 120K protein in amoebae of Dictyostelium discoideum. J. Cell Biol. 100:1884–1893.
   PubMedGoogle Scholar
• Cheung, W. Y.. 1980. Calmodulin plays a pivotal role in cellular regulation. Science 207:19–27.
   PubMed Web of Science ®Google Scholar
• Chisholm, R. L., A. M. Rushforth, R. S. Pollenz, E. R. Kuczmarski, and S. R. Tafuri. 1988. Dictyostelium discoideiun myosin: isolation and characterization of cDNAs encoding the essential light chain. Mol. Cell. Biol. 8:794–810.
   PubMedGoogle Scholar
• Clark, M., and J. A. Spudich. 1974. Biochemical and structural studies of actomyosin-like proteins from non-muscle cells. J. Mol. Biol. 86:209–222.
   PubMedGoogle Scholar
• Collins, J. H.. 1976. Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbumin. Nature (London) 259:699–700.
   PubMed Web of Science ®Google Scholar
• Cote, G. P., J. P. Albanesi, I. Ueno, J. A. Hammer III, and E. D. Korn. 1985. Purification from Dictyosteliun discoidium of a low-molecular-weight myosin that resembles myosin I from Acanthamoeba castellanii. J. Biol. Chem. 260:4543–4546.
   PubMedGoogle Scholar
• Craig, R., R. Smith, and J. Kendrick-Jones. 1983. Light chain phosphorylation controls the conformation of vertebrate nonmuscle and smooth muscle myosin molecules. Nature (London) 302:436–439.
   PubMedGoogle Scholar
• Daniel, J. L., I. R. Molish, and H. Holmsen. 1981. Myosin phosphorylation in intact platelets. J. Biol. Chem. 256:7510–7514.
   PubMedGoogle Scholar
• Daniel, J. L., I. R. Molish, M. Rigmaiden, and G. Stewart. 1984. Evidence for a role of myosin phosphorylation in the initiation of the platelet shape change response. J. Biol. Chem. 259:9826–9831.
   PubMed Web of Science ®Google Scholar
• De Lozanne, A., and J. A. Spudich. 1987. Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236:1086–1091.
   PubMed Web of Science ®Google Scholar
• Devereux, J., P. Haeberti, and O. Smithes. 1984. A comprehensive set of sequence analysis programs for the Vax. Nucleic Acids Res. 12:387–395.
   PubMed Web of Science ®Google Scholar
• Feinberg, A., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6–13.
   PubMed Web of Science ®Google Scholar
• Feinberg, A., and B. Vogelstein. 1984. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 137:266–267.
   PubMed Web of Science ®Google Scholar
• Fujiwara, K., and T. D. Pollard. 1976. Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells. J. Cell Biol. 71:848–875.
   PubMed Web of Science ®Google Scholar
• Griffith, L. M., S. M. Downs, and J. A. Spudich. 1987. Myosin light chain kinase and myosin light chain phosphatase from Dictyostelium: effects of reversible phosphorylation on myosin structure and function. J. Cell Biol. 104:1309–1323.
   PubMedGoogle Scholar
• Harrington, W. F., and E. Rogers. 1984. Myosin. Annu. Rev. Biochem. 53:35–73.
   PubMed Web of Science ®Google Scholar
• Kemp, B. E., and R. B. Pearson. 1985. Spatial requirements for location of basic residues in peptide substrates for smooth muscle myosin light chain kinase. J. Biol. Chem. 260:3355–3359.
   PubMed Web of Science ®Google Scholar
• Kemp, B. E., R. B. Pearson, and C. House. 1982. Phosphorylation of a synthetic heptapeptide by smooth muscle myosin light chain kinase. J. Biol. Chem. 257:13349–13353.
   PubMedGoogle Scholar
• Kemp, B. E., R. B. Pearson, and C. House. 1983. Role of basic residues in the phosphorylation of synthetic peptides by myosin light chain kinase. Proc. Natl. Acad. Sci. USA 80:7471–7475.
   PubMedGoogle Scholar
• Kendrick-Jones, J., and J. M. Scholey. 1981. Myosin-linked regulatory systems. J. Muscle Res. Cell Motil. 2:347–372.
   Web of Science ®Google Scholar
• Kerrick, W. G., and L. W. Bourguignon. 1984. Regulation of receptor capping in mouse lymphoma T cells by a Ca+2- activated myosin light chain kinase. Proc. Natl. Acad. Sci. USA 81:165–169.
   PubMedGoogle Scholar
• Kimmel, A. R., and R. A. Firtel. 1982. The organization and expression of the Dictyostelium genome, p. 234–324. In W. F. Loomis (ed.). The development of Dictyostelium discoidium. Academic Press, Inc., New York.
   Google Scholar
• Kimmel, A. R., and R. A. Firtel. 1983. Sequence organization in Dictyostelium: unique structure at the 5′ ends of protein coding genes. Nucleic Acids Res. 11:541–552.
   PubMedGoogle Scholar
• Knecht, D. A., and W. F. Loomis. 1987. Anti-sense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideiun. Science 236:1081–1086.
   PubMed Web of Science ®Google Scholar
• Knecht, D. A., and W. F. Loomis. 1988. Developmental consequences of the lack of myosin heavy chain in Dictyostelium discoidium. Dev. Biol. 128:178–184.
   PubMedGoogle Scholar
• Kretsinger, R. H.. 1980. Structure and evolution of calcium modulated proteins. Crit. Rev. Biochem. 8:119–174.
   PubMed Web of Science ®Google Scholar
• Kuczmarski, E. R.. 1986. Partial purification of two myosin heavy chain kinases from Dictyostelium discoidium. J. Muscle Res. Cell Motil. 7:501–509.
   PubMedGoogle Scholar
• Kuczmarski, E. R., and J. A. Spudich. 1980. Regulation of myosin self-assembly: phosphorylation of Dictyostelium heavy chain inhibits formation of thick filaments. Proc. Natl. Acad. Sci. USA 77:7292–7296.
   PubMedGoogle Scholar
• Kumar, C. C., L. Cribbs, P. Delaney, K. R. Chien, and M. A. Q. Siddiqui. 1986. Heart myosin light chain 2 gene. J. Biol. Chem. 261:2866–2872.
   PubMedGoogle Scholar
• Kuznicki, J., and B. Barylko. 1988. Phosphorylation of myosin in smooth muscle and non-muscle cells: in vitro and in vivo effects. Int. J. Biochem. 20:559–568.
   PubMedGoogle Scholar
• Lacombe, M. L., G. J. Podgorski, J. Franke, and R. H. Kessin. 1986. Molecular cloning and developmental expression of the cyclic nucleotide phosphodiesterase gene from Dictyostelium discoideiun. J. Biol. Chem. 261:16811–16817.
   PubMedGoogle Scholar
• Maniatis, T., E. F. Fritsch, and J. Sam brook. 1980. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Maruta, H., W. Bates, P. Dieter, D. Marme, and G. Gerisch. 1983. Myosin heavy chain kinase inactivated by Ca+2/calmod- ulin from aggregating cells of Dictyostelium discoidium. EMBO J. 2:535–542.
   PubMedGoogle Scholar
• Maruta, H., H. Gadasi, J. H. Collins, and E. D. Korn. 1978. The isolated heavy chain of an Acanthamoeba myosin contains full enzymatic activity. J. Biol. Chem. 253:6297–6300.
   PubMed Web of Science ®Google Scholar
• Nellen, W., C. Silan, and R. A. Firtel. 1984. DNA-mediated transformation in Dictyostelium discoideiun: regulated expression of an actin gene fusion. Mol. Cell. Biol. 4:2890–2898.
   PubMedGoogle Scholar
• Okomoto, Y., T. Sekine, J. Grammer, and R. G. Yount. 1986. The essential light chains constitute part of the active site of smooth muscle myosin. Nature (London) 324:78–80.
   PubMedGoogle Scholar
• Pearson, R. B., L. Y. Misconi, and B. E. Kemp. 1986. Smooth muscle myosin kinase requires residues on the COOH-terminal side of the phosphorylation site. J. Biol. Chem. 261:25–27.
   PubMed Web of Science ®Google Scholar
• Persechini, A., and D. J. Hartshorne. 1981. Phosphorylation of smooth muscle myosin: evidence for cooperativity between the myosin heads. Science 213:1383–1385.
   PubMed Web of Science ®Google Scholar
• Peters, D. J. M., D. A. Knecht, W. F. Loomis, A. De Lozanne, J. A. Spudich, and P. J. M. Van Hastert. 1988. Signal transduction. chemotaxis, and cell aggregation in Dictyostelium discoidium cells without myosin heavy chain. Dev. Biol. 128:158–163.
   PubMedGoogle Scholar
• Pollard, T. D., and K. Fujiwara. 1976. Participation of contractile proteins in cytoplasmic structure and cell division, p. 23–28. In S. V. Perry, A. Margreth, and R. S. Adelstein (ed.). Contractile systems in non-muscle tissues. North-Holland Publishing Co., Amsterdam.
   Google Scholar
• Prince, H. P., H. R. Trayer, G. D. Henry, I. P. Trayer, and D. C. Dalgarno. 1981. Proton nuclear-magnetic-resonance spectroscopy of myosin subfragment I isoenzymes. Eur. J. Biochem. 121:213–219.
   PubMedGoogle Scholar
• Pustell, J., and F. C. Kafatos. 1984. A convenient and adaptable package of computer programs for DNA and protein sequence management, analysis and homology determination. Nucleic Acids Res. 12:643–655.
   PubMedGoogle Scholar
• Rappaport, R.. 1967. Cell division: direct measurement of maximum tension exerted by furrow of echinoderm eggs. Science 156:1241–1242.
   PubMed Web of Science ®Google Scholar
• Reed, K. C., and D. A. Mann. 1985. Rapid transfer of DNA from agarose gels to nylon membranes. Nucleic Acids Res. 13:7202–7221.
   Google Scholar
• Reinach, F. C., K. Nagai, and J. Kendrick-Jones. Site-directed mutagenesis of the regulatory light-chain Ca+2/Mg+2 binding site and its role in hybrid myosins. Nature (London) 322:80–83.
   Google Scholar
• Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Schliwa, M.. 1984. Mechanisms of intracellular organelle transport, p. 1–82. In J. W. Shay (ed.). Cell and muscle motility: the cytoskeleton. Plenum Publishing Corp., New York.
   Google Scholar
• Scholey, J. M., R. C. Smith, D. Drenckhahn, U. Groschel-Stewart, and J. Kendrick-Jones. 1982. Thymus myosin. J. Biol. Chem. 257:7737–7745.
   PubMed Web of Science ®Google Scholar
• Schroeder, T. E.. 1972. The contractile ring. II. Determining its brief existence, volumetric changes, and vital role in cleaving arbacia eggs. J. Cell Biol. 53:419–434.
   PubMed Web of Science ®Google Scholar
• Schroeder, T. E.. 1973. Actin in dividing cells: contractile ring filaments bind heavy meromyosin. Proc. Natl. Acad. Sci. USA 70:1688–1692.
   PubMedGoogle Scholar
• Senda, N.. 1976. The movement of leucocytes, p. 309–323. In S. V. Perry, A. Margreth, and R. S. Adelstein (ed.), Contractile systems of non-muscle tissues. North-Holland Publishing Co., Amsterdam.
   Google Scholar
• Sivaramakrishnan, M., and M. Burke. 1982. The free heavy chain of vertebrate skeletal myosin subfragment 1 shows full enzymatic activity. J. Biol. Chem. 257:1102–1105.
   PubMedGoogle Scholar
• Sobieszek, A., and J. V. Small. 1977. Regulation of the actinmyosin interaction in vertebrate smooth muscle: activation via a myosin light chain kinase and the effect of tropomyosin. J. Mol. Biol. 112:559–576.
   PubMed Web of Science ®Google Scholar
• Spudich, J. A.. 1974. Biochemical and structural studies of actomyosin like proteins from non-muscle cells. J. Biol. Chem. 249:6013–6020.
   PubMedGoogle Scholar
• Stossel, T. P., and J. H. Hartwig. 1976. Phagocytosis and the contractile proteins of pulmonary macrophages, p. 529–544. In R. Goldman, T. Pollard, and J. Rosenbaum (ed.). Cell motility. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Vaillancourt, J. P., C. Lyons, and G. P. Cote. 1988. Identification of two phosphorylated threonines in the tail region of Dictyostelium myosin II. J. Biol. Chem. 263:10082–10087.
   PubMedGoogle Scholar
• Varnum, B., and D. R. Soil. 1984. Effects of cAMP on single cell motility. J. Cell Biol. 99:1151–1155.
   PubMed Web of Science ®Google Scholar
• Wagner, P. D., and E. Giniger. 1981. Hydrolysis of ATP and reversible binding to F-actin by myosin heavy chains free of all light chains. Nature (London) 292:560–562.
   PubMedGoogle Scholar
• Warrick, H. M., A. De Lozanne, L. A. Leinwand, and J. A. Spudich. 1986. Conserved protein domains in a myosin heavy chain gene from Dictvostelium discoideum. Proc. Natl. Acad. Sci. USA 83:9422–9437.
   Google Scholar
• Weinberger, C., S. M. Hollenberg, E. S. Ong, J. M. Harmon, S. T. Brower, J. Cidlowski, E. B. Thompson, M. G. Rosenfeld, and R. M. Evans. 1985. Identification of human glucocorticoid receptor cDNA clones by epitope selection. Science 228:740–742.
   PubMedGoogle Scholar
• Wessels, D., D. R. Soll, D. A. Knecht, W. F. Loomis, A. De Lozanne, and J. A. Spudich. 1988. Cell motility and chemotaxis in Dictvostelium amoeba lacking myosin heavy chain. Dev. Biol. 128:164–177.
   PubMedGoogle Scholar
• Witke, W., W. Nellen, and A. Noegel. 1987. Homologous recombination in the Dictyostelium a-actin in gene leads to an altered mRNA and lack of protein. EMBO J. 6:4143–4148.
   PubMedGoogle Scholar
• Young, R. A., and R. W. Davis. 1983. Efficient isolation of genes by using antibody probes. Proc. Natl. Acad. Sci. USA 80:1194–1198.
   PubMed Web of Science ®Google Scholar
• Yumura, S., and Y. Fukui. 1985. Reversible cyclic AMPdependent change in distribution of myosin thick filaments in Dictyostelium. Nature (London) 314:194–196.
   PubMedGoogle Scholar
• Yumura, S., H. Mori, and Y. Fukui. 1984. Localization of actin and myosin for the study of ameboid movement in Dictyostelium using improved immunofluorescence. J. Cell Biol. 99:894–899.
   PubMed Web of Science ®Google Scholar