| Literature DB >> 29248727 |
Sa Rula1, Takahiro Suwa1, Saku T Kijima2, Takeshi Haraguchi1, Shinryu Wakatsuki1, Naruki Sato1, Zhongrui Duan3, Motoki Tominaga4, Taro Q P Uyeda5, Kohji Ito6.
Abstract
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.Entities:
Keywords: Actin; Arabidopsis; Cytoplasmic streaming; Myosin
Mesh:
Substances:
Year: 2017 PMID: 29248727 DOI: 10.1016/j.bbrc.2017.12.071
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575