J. Biochem, 1989, Vol. 106, No. 1 172-180
© 1989 Japanese Biochemical Society
research-article |
An Actin-Depolymerizing Protein in Embryonic Chicken Skeletal Muscle: Purification and Characterization1
*Graduate School of Science and Technology, Chiba University Chiba, Chiba 260
**Department of Biology, Chiba University Chiba, Chiba 260
2To whom correspondence should be addressed.
In embryonic skeletal muscle, a large amount of non-polymerized actin exists in the cytoplasm (Shimizu and Obinata [1986] J. Biochem. 99, 751–759). A 19-kDa protein (called 19K protein) which binds to G-actin was purified by sequential chromatography on DNase I-agarose, hydroxylapatite, SP-Sephadex, and Sephadex G-75, from the sarcoplasmic fraction of embryonic chicken skeletal muscle. This protein decreased the extent of actin polymerization at a steady state and increased the monomeric actin in a concentration-dependent fashion; it also caused quick depolymerization of F-actin, as determined by spectrophotometry at 237 nm, viscometry, DNase I inhibition assay, and electron microscopy. The molar ratio of 19K protein and actin interacting with each other was estimated to be 1: 1. From these results, 19K protein was regarded as being actin depolymerizing protein. The amount of 19K protein in muscle decreased during development. The inhibitory action of 19K protein was removed by myosin or heavy meromyosin, and actin filaments were formed on the surface of myosin filaments when myosin filaments were added to a mixture of actin and 19K protein in a physiological salt solution. We propose that actin assembly is dually controlled in the developing muscle by the inhibitor(s) and an accelerator (myosin); this mechanism may enable the ordered assembly of actin and myosin in the early phase of myofibrillogenesis.
1This work was supported in part by grants from the Shimadzu Science Foundation, the Ministry of Education, Science and Culture, the Ministry of Health and Welfare of Japan, and the Muscular Dystrophy Association of America.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  K. Nakashima, N. Sato, T. Nakagaki, H. Abe, S. Ono, and T. Obinata Two Mouse Cofilin Isoforms, Muscle-Type (MCF) and Non-Muscle Type (NMCF), Interact with F-Actin with Different Efficiencies J. Biochem., October 1, 2005; 138(4): 519 - 526. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Ono, M. Parast, C. Alberico, G. M. Benian, and S. Ono Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans J. Cell Sci., May 15, 2003; 116(10): 2073 - 2085. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M.-F. Carlier, F. Ressad, and D. Pantaloni Control of Actin Dynamics in Cell Motility. ROLE OF ADF/COFILIN J. Biol. Chem., November 26, 1999; 274(48): 33827 - 33830. [Full Text] [PDF]
|
|
|
|
 |
|
 S. Ono, D. L. Baillie, and G. M. Benian UNC-60B, an ADF/Cofilin Family Protein, Is Required for Proper Assembly of Actin into Myofibrils in Caenorhabditis elegans Body Wall Muscle J. Cell Biol., May 3, 1999; 145(3): 491 - 502. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Ono and G. M. Benian Two Caenorhabditis elegans Actin Depolymerizing Factor/Cofilin Proteins, Encoded by the unc-60 Gene, Differentially Regulate Actin Filament Dynamics J. Biol. Chem., February 6, 1998; 273(6): 3778 - 3783. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M.-F. Carlier, V. Laurent, J. Santolini, R. Melki, D. Didry, G.-X. Xia, Y. Hong, N.-H. Chua, and D. Pantaloni Actin Depolymerizing Factor (ADF/Cofilin) Enhances the Rate of Filament Turnover: Implication in Actin-based Motility J. Cell Biol., March 24, 1997; 136(6): 1307 - 1322. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R Nagaoka, K Kusano, H Abe, and T Obinata Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action J. Cell Sci., January 2, 1995; 108(2): 581 - 593. [Abstract] [PDF]
|
|