Abstract
A protein fraction from the cellular slime mold Dictyostelium discoideum confers Ca2+-sensitivity on the activation of purified myosin adenosinetriphosphatase (ATP phosphohydrolase, EC 3.6.1.3) from Dictyostelium by purified Dictyostelium actin. That is, the fraction inhibits the actomyosin adenosine triphosphatase activity in the absence of Ca+ but not in the presence of Ca2+. This Ca2+-sensitizing factor affects only the actin-activated myosin adenosine triphosphatase and not the enzyme activity of myosin alone. The Ca2+-sensitivity is conserved when muscle actin replaces Dictyostelium actin, but is lost when muscle myosin replaces Dictyostelium myosin. The factor appears to be a protein since it is nondialyzable, is heat labile, and can be precipitated with ammonium sulfate. The factor can be purified 70-fold on an actin-affinity column.
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- Ames G. F. Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions. J Biol Chem. 1974 Jan 25;249(2):634–644. [PubMed] [Google Scholar]
- Arnold H., Pette D. Binding of glycolytic enzymes to structure proteins of the muscle. Eur J Biochem. 1968 Nov;6(2):163–171. doi: 10.1111/j.1432-1033.1968.tb00434.x. [DOI] [PubMed] [Google Scholar]
- Clarke M., Spudich J. A. Biochemical and structural studies of actomyosin-like proteins from non-muscle cells. Isolation and characterization of myosin from amoebae of Dictyostelium discoideum. J Mol Biol. 1974 Jun 25;86(2):209–222. doi: 10.1016/0022-2836(74)90013-8. [DOI] [PubMed] [Google Scholar]
- Cohen I., Cohen C. A tropomyosin-like protein from human platelets. J Mol Biol. 1972 Jul 21;68(2):383–387. doi: 10.1016/0022-2836(72)90220-3. [DOI] [PubMed] [Google Scholar]
- Cohen I., Kaminski E., De Vries A. Actin-linked regulation of the human platelet contractile system. FEBS Lett. 1973 Aug 15;34(2):315–317. doi: 10.1016/0014-5793(73)80820-8. [DOI] [PubMed] [Google Scholar]
- Fine R. E., Blitz A. L., Hitchcock S. E., Kaminer B. Tropomyosin in brain and growing neurones. Nat New Biol. 1973 Oct 10;245(145):182–186. doi: 10.1038/newbio245182a0. [DOI] [PubMed] [Google Scholar]
- Hartree E. F. Determination of protein: a modification of the Lowry method that gives a linear photometric response. Anal Biochem. 1972 Aug;48(2):422–427. doi: 10.1016/0003-2697(72)90094-2. [DOI] [PubMed] [Google Scholar]
- Hatano S. Specific effect of Ca2+ on movement of plasmodial fragment obtained by caffeine treatment. Exp Cell Res. 1970 Jul;61(1):199–203. doi: 10.1016/0014-4827(70)90274-0. [DOI] [PubMed] [Google Scholar]
- Jahn T. L., Bovee E. C. Protoplasmic movements within cells. Physiol Rev. 1969 Oct;49(4):793–862. doi: 10.1152/physrev.1969.49.4.793. [DOI] [PubMed] [Google Scholar]
- Kato T., Tonomura Y. Ca2+-sensitivity of actomyosin ATPase purified from Physarum polycephalum. J Biochem. 1975 Jun;77(6):1127–1134. [PubMed] [Google Scholar]
- Kato T., Tonomura Y. Physarum tropomyosin-troponin complex. Isolation and properties. J Biochem. 1975 Sep;78(3):583–588. doi: 10.1093/oxfordjournals.jbchem.a130943. [DOI] [PubMed] [Google Scholar]
- Kendrick-Jones J. Role of myosin light chains in calcium regulation. Nature. 1974 Jun 14;249(458):631–634. doi: 10.1038/249631a0. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lazarides E., Lindberg U. Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4742–4746. doi: 10.1073/pnas.71.12.4742. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mason J. W., Rasmussen H., Dibella F. 3'5' AMP and Ca 2+ in slime mold aggregation. Exp Cell Res. 1971 Jul;67(1):156–160. doi: 10.1016/0014-4827(71)90631-8. [DOI] [PubMed] [Google Scholar]
- Nachmias V., Asch A. Actin mediated calcium dependency of actomyosin in a myxomycete. Biochem Biophys Res Commun. 1974 Sep 23;60(2):656–664. doi: 10.1016/0006-291x(74)90291-5. [DOI] [PubMed] [Google Scholar]
- Pollard T. D., Eisenberg E., Korn E. D., Kielley W. W. Inhibition of Mg ++ ATPase activity of actin-activated Acanthamoeba myosin by muscle troponin-tropomyosin: implications for the mechanism of control of amoeba motility and muscle contraction. Biochem Biophys Res Commun. 1973 Apr 2;51(3):693–698. doi: 10.1016/0006-291x(73)91370-3. [DOI] [PubMed] [Google Scholar]
- Pollard T. D., Weihing R. R. Actin and myosin and cell movement. CRC Crit Rev Biochem. 1974 Jan;2(1):1–65. doi: 10.3109/10409237409105443. [DOI] [PubMed] [Google Scholar]
- Richards E. G., Chung C. S., Menzel D. B., Olcott H. S. Chromatography of myosin on diethylaminoethyl-Sephadex A-50. Biochemistry. 1967 Feb;6(2):528–540. doi: 10.1021/bi00854a022. [DOI] [PubMed] [Google Scholar]
- Shibata N., Tatsumi N., Tanaka K., Okamura Y., Senda N. A contractile protein possessing Ca 2+ sensitivity (natural actomyosin) from leucocytes. Its extraction and some of its properties. Biochim Biophys Acta. 1972 Feb 28;256(2):565–576. doi: 10.1016/0005-2728(72)90084-9. [DOI] [PubMed] [Google Scholar]
- Spudich J. A. Biochemical and structural studies of actomyosin-like proteins from non-muscle cells. II. Purification, properties, and membrane association of actin from amoebae of Dictyostelium discoideum. J Biol Chem. 1974 Sep 25;249(18):6013–6020. [PubMed] [Google Scholar]
- Spudich J. A., Cooke R. Supramolecular forms of actin from amoebae of Dictyostelium discoideum. J Biol Chem. 1975 Sep 25;250(18):7485–7491. [PubMed] [Google Scholar]
- Spudich J. A., Watt S. 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. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
- Szent-Györgyi A. G., Szentkiralyi E. M., Kendrick-Jonas J. The light chains of scallop myosin as regulatory subunits. J Mol Biol. 1973 Feb 25;74(2):179–203. doi: 10.1016/0022-2836(73)90106-x. [DOI] [PubMed] [Google Scholar]
- Tanaka H., Hatano S. Extraction of native tropomyosin-like substances from myxomycete plasmodium and the cross reaction between plasmodium F-actin and muscle native tropomyosin. Biochim Biophys Acta. 1972 Feb 29;257(2):445–451. doi: 10.1016/0005-2795(72)90297-8. [DOI] [PubMed] [Google Scholar]
- Taylor D. L., Condeelis J. S., Moore P. L., Allen R. D. The contractile basis of amoeboid movement. I. The chemical control of motility in isolated cytoplasm. J Cell Biol. 1973 Nov;59(2 Pt 1):378–394. doi: 10.1083/jcb.59.2.378. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tonomura Y., Appel P., Morales M. On the molecular weight of myosin. II. Biochemistry. 1966 Feb;5(2):515–521. doi: 10.1021/bi00866a017. [DOI] [PubMed] [Google Scholar]
- Weber A., Murray J. M. Molecular control mechanisms in muscle contraction. Physiol Rev. 1973 Jul;53(3):612–673. doi: 10.1152/physrev.1973.53.3.612. [DOI] [PubMed] [Google Scholar]
- Wessells N. K., Spooner B. S., Ash J. F., Bradley M. O., Luduena M. A., Taylor E. L., Wrenn J. T., Yamada K. Microfilaments in cellular and developmental processes. Science. 1971 Jan 15;171(3967):135–143. doi: 10.1126/science.171.3967.135. [DOI] [PubMed] [Google Scholar]