Abstract
Plasmodial fragments of Physarum polycephalum, excised from anterior regions of a thin-spread plasmodium, contracted-relaxed cyclicly with a period of 3-5 min. The area of the fragments decreased approximately 10% during contraction. In most cases, there was little endoplasmic streaming which indicates that contractions were synchronized throughout the fragment. By both polarized light and fluorescence microscopy, the organization and distribution of the cytoplasmic actomyosin fibrils in the fragments changed in synchrony with the contraction cycle. The fibrils formed during the contraction phase, and finally became a highly organized framework consisting of a three- dimensional network of numerous fibrils with many converging points (the nodes). During relaxation, the fibrils degenerated and disappeared almost completely, though some very weak fibrils remained near the nodes and the periphery. The results obtained by fluorometry of the fragments, stained with rhodamine-phalloidin, suggested that the G-F transformation of actin is not the main underlying process of the fibrillar formation.
Full Text
The Full Text of this article is available as a PDF (1.6 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Achenbach F., Wohlfarth-Bottermann K. E. Reactivation of cell-free models of endoplasmic drops from Physarum polycephalum after glycerol extraction at low ionic strength. Eur J Cell Biol. 1986 Apr;40(2):135–138. [PubMed] [Google Scholar]
- Brugmans M., Cassiman J. J., van den Berghe H. Selective adhesion and impaired adhesive properties of transformed cells. J Cell Sci. 1978 Oct;33:121–132. doi: 10.1242/jcs.33.1.121. [DOI] [PubMed] [Google Scholar]
- Buckley I. K., Porter K. R. Cytoplasmic fibrils in living cultured cells. A light and electron microscope study. Protoplasma. 1967;64(4):349–380. doi: 10.1007/BF01666538. [DOI] [PubMed] [Google Scholar]
- Hasegawa T., Takahashi S., Hayashi H., Hatano S. Fragmin: a calcium ion sensitive regulatory factor on the formation of actin filaments. Biochemistry. 1980 Jun 10;19(12):2677–2683. doi: 10.1021/bi00553a021. [DOI] [PubMed] [Google Scholar]
- Isenberg G., Wohlfarth-Bottermann K. E. Transformation of cytoplasmic actin. Importance for the organization of the contractile gel reticulum and the contraction--relasation cycle of cytoplasmic actomyosin. Cell Tissue Res. 1976 Oct 19;173(4):495–528. doi: 10.1007/BF00224311. [DOI] [PubMed] [Google Scholar]
- Kessler D. On the location of myosin in the myxomycete Physarum polycephalum and its possible function in cytoplasmic streaming. J Mechanochem Cell Motil. 1972 Aug;1(3):125–137. [PubMed] [Google Scholar]
- Kuroda R., Kuroda H. Relation of cytoplasmic calcium to contractility in Physarum polycephalum. J Cell Sci. 1982 Feb;53:37–48. doi: 10.1242/jcs.53.1.37. [DOI] [PubMed] [Google Scholar]
- Lazarides E. Actin, alpha-actinin, and tropomyosin interaction in the structural organization of actin filaments in nonmuscle cells. J Cell Biol. 1976 Feb;68(2):202–219. doi: 10.1083/jcb.68.2.202. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lazarides E., Burridge K. Alpha-actinin: immunofluorescent localization of a muscle structural protein in nonmuscle cells. Cell. 1975 Nov;6(3):289–298. doi: 10.1016/0092-8674(75)90180-4. [DOI] [PubMed] [Google Scholar]
- Lazarides E., Weber K. Actin antibody: the specific visualization of actin filaments in non-muscle cells. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2268–2272. doi: 10.1073/pnas.71.6.2268. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ogihara S., Ikebe M., Takahashi K., Tonomura Y. Requirement of phosphorylation of Physarum myosin heavy chain for thick filament formation, actin activation of Mg2+-ATPase activity, and Ca2+-inhibitory superprecipitation. J Biochem. 1983 Jan;93(1):205–223. doi: 10.1093/oxfordjournals.jbchem.a134155. [DOI] [PubMed] [Google Scholar]
- Ogihara S., Tonomura Y. A novel 36,000-dalton actin-binding protein purified from microfilaments in Physarum plasmodia which aggregates actin filaments and blocks actin-myosin interaction. J Cell Biol. 1982 Jun;93(3):604–614. doi: 10.1083/jcb.93.3.604. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pies N. J., Wohlfarth-Bottermann K. E. Reactivation of a cell-free model from Physarum polycephalum: studies on cryosections indicate an inhibitory effect of Ca++ on cytoplasmic actomyosin contraction. Eur J Cell Biol. 1986 Apr;40(2):139–149. [PubMed] [Google Scholar]
- Ueda T., Matsumoto K., Akitaya T., Kobatake Y. Spatial and temporal organization of intracellular adenine nucleotides and cyclic nucleotides in relation to rhythmic motility in Physarum plasmodium. Exp Cell Res. 1986 Feb;162(2):486–494. doi: 10.1016/0014-4827(86)90352-6. [DOI] [PubMed] [Google Scholar]
- Wohlfarth-Bottlermann K. E., Fleischer M. Cycling aggregation patterns of cytoplasmic F-actin coordinated with oscillating tension force generation. Cell Tissue Res. 1976 Jan 27;165(3):327–344. doi: 10.1007/BF00222437. [DOI] [PubMed] [Google Scholar]
- Yoshimoto Y., Kamiya N. ATP- and calcium-controlled contraction in a saponin model of Physarum polycephalum. Cell Struct Funct. 1984 Jun;9(2):135–141. doi: 10.1247/csf.9.135. [DOI] [PubMed] [Google Scholar]
- Yoshimoto Y., Matsumura F., Kamiya N. Simultaneous oscillations of Ca2+ efflux and tension generation in the permealized plasmodial strand of Physarum. Cell Motil. 1981;1(4):433–443. doi: 10.1002/cm.970010404. [DOI] [PubMed] [Google Scholar]