Tetrahymena actin: copolymerization with skeletal muscle actin and interactions with muscle actin-binding proteins.
We have previously shown that actin from Tetrahymena pyriformis has a very divergent primary structure (Hirono, M., Endoh, H., Okada, N., Numata, O., & Watanabe, Y. (1987) J. Mol. Biol. 194, 181-192) and that though it shares essential properties with skeletal muscle actin, it does not interact at all with phalloidin or DNase I (Hirono, M., Kumagai, Y., Numata, O., & Watanabe, Y. (1989) Proc. Natl. Acad. Sci. U.S. 86, 75-79). In this study, we investigated the copolymerization of this actin with skeletal muscle actin by direct observation of the heteropolymers formed from the two actins by means of electron microscopy. We also examined the binding of actin-binding proteins from skeletal muscle or smooth muscle to Tetrahymena actin by means of a cosedimentation assay. The results show that (i) Tetrahymena actin copolymerizes with skeletal muscle actin and that (ii) muscle myosin subfragment 1 binds to it in the absence of ATP, like skeletal muscle actin. However, it was also shown that (iii) muscle alpha-actinin hardly binds to Tetrahymena actin and that (iv) muscle tropomyosin does not bind to it at all. The results show that Tetrahymena actin has both properties similar and dissimilar to those of skeletal muscle actin.
Hirono
M
M
Institute of Biological Sciences, University of Tsukuba, Ibaraki.
Tanaka
R
R
Watanabe
Y
Y
D000185:Actinin / Q000378:metabolism*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D001704:Biopolymers; D002645:Chickens; D009132:Muscles / Q000032:analysis*; D011485:Protein Binding; D011817:Rabbits; D013769:Tetrahymena pyriformis / Q000032:analysis*; D014335:Tropomyosin / Q000378:metabolism*
D000199:Actins; D001704:Biopolymers; D014335:Tropomyosin; D000185:Actinin