Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiol, October 1999, Vol. 121, pp. 525-534

Biochemical and Immunocytochemical Characterization of Two Types of Myosins in Cultured Tobacco Bright Yellow-2 Cells1

Etsuo Yokota,* Chiharu Yukawa,2 Shoshi Muto, Seiji Sonobe, and Teruo Shimmen

Department of Life Science, Faculty of Science, Himeji Institute of Technology, Harima Science Park City, Hyogo 678-12, Japan (E.Y., C.Y., S.S., T.S.); and Bio-Science Center, Nagoya University, Nagoya 464-01, Japan (S.M.)

We have isolated a myosin (referred to as 170-kD myosin) from lily pollen tubes, which consists of 170-kD heavy chain and calmodulin (CaM) light chain and is responsible for cytoplasmic streaming. A 170-kD polypeptide that has similar antigenicity to the 170-kD myosin heavy chain of lily pollen tubes was also present in cultured tobacco (Nicotiana tabacum) Bright Yellow-2 (BY-2) cells, and possessed the ability to interact with F-actin in an ATP-dependent manner. In addition to this myosin, we identified biochemically another kind of myosin in BY-2 cells. This myosin consisted of a CaM light chain and a 175-kD heavy chain with antigenicity different from the 170-kD myosin heavy chain. In the present study, we referred to this myosin as 175-kD myosin. This myosin was able to translocate rhodamine-phalloidin (RP)-labeled F-actin at an average velocity of about 9 µm/s in the motility assay in vitro. In contrast, the sliding velocity of RP-labeled F-actin translocated by fractions containing the 170-kD myosin was 3 to 4 µm/s. The velocity of cytoplasmic streaming in living BY-2 cells ranged from 2 to 9 µm/s. The motile activity of 175-kD myosin in vitro was inhibited by Ca2+ at concentrations higher than 10-6 M. Immunoblot analyses using an antiserum against the heavy chain of 170- or 175-kD myosin revealed that in tobacco plants, the 175-kD myosin was expressed in leaf, stem, and root, but not in germinating pollen, while 170-kD myosin was present in all of these plant parts and in germinating pollen. These results suggest that the two types of myosins, 170 and 175 kD, presumably participate in cytoplasmic streaming in BY-2 cells and other somatic cells of tobacco plants.

1 This work was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (grant no. 09740602 to E.Y.).

2 Present address: Sawada Menko, Himeji, Hyogo 670, Japan.

* Corresponding author; e-mail yokota{at}sci.himeji-tech.ac.jp; fax 791-58-0175.

© 1999 American Society of Plant Physiologists


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