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Measurement of enzymatic and motile activities of Arabidopsis myosins by using Arabidopsis actins

Journal Article · · Biochemical and Biophysical Research Communications
;  [1];  [2]; ; ;  [1];  [3];  [3];  [2];  [1]
  1. Department of Biology, Graduate School of Science, Chiba University, Inage-ku, Chiba 263-8522 (Japan)
  2. Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Ibaraki 305-8565 (Japan)
  3. Faculty of Education and Integrated Arts and Sciences, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480 (Japan)
Highlights: • Enzymatic activities of Arabidopsis myosins are measured by using Arabidopsis actin isoforms. • Motile activities of Arabidopsis myosins are measured by using Arabidopsis actin isoforms. • These values are different from those measured by using animal muscle actin isoforms. • Arabidopsis myosins show different activities when using different Arabidopsis actin isoforms. There are two classes of myosin, XI and VIII, in higher plants. Myosin XI moves actin filaments at high speed and its enzyme activity is also very high. In contrast, myosin VIII moves actin filaments very slowly with very low enzyme activity. Because most of these enzymatic and motile activities were measured using animal skeletal muscle α-actin, but not plant actin, they would not accurately reflect the actual activities in plant cells. We thus measured enzymatic and motile activities of the motor domains of two Arabidopsis myosin XI isoforms (MYA2, XI-B), and one Arabidopsis myosin VIII isoform (ATM1), by using three Arabidopsis actin isoforms (ACT1, ACT2, and ACT7). The measured activities were different from those measured by using muscle actin. Moreover, Arabidopsis myosins showed different enzymatic and motile activities when using different Arabidopsis actin isoforms. Our results suggest that plant actin should be used for measuring enzymatic and motile activities of plant myosins and that different actin isoforms in plant cells might function as different tracks along which affinities and velocities of each myosin isoform are modulated.
OSTI ID:
23127471
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 3 Vol. 495; ISSN 0006-291X; ISSN BBRCA9
Country of Publication:
United States
Language:
English

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