J. Biochem, 1992, Vol. 112, No. 6 786-791
© 1992 Japanese Biochemical Society
research-article |
Isolation of cDNA for Bovine Stomach 155 kDa Protein Exhibiting Myosin Light Chain Kinase Activity1
*Department of Physics, Faculty of Science, The University of Tokyo Bunhyo-ky Tokyo 113
**Department of Pharmacology, Institute of Basic Medical sciences, University of Tsukuba Tsukuba, Ibaraki 305
***National Institute for Physiological Sciences Okazaki, Aichi 444
****Division of Cellar Communication, Department of Cellular Biology, National Institute for Basic Biology Okazaki, Aichi 444
6To whom all correspondence should be addressed
Two proteins with myosin light chain kinase activity and electrophoretic molecular weights of 155,000 and 130,000 were each isolated from bovine stomach smooth muscle [Kuwayama, H., Suzuki, M., Koga, R., & Ebashi, S. (1988) J. Biochem 104, 862–866]. The 155 kDa component showed a much higher superprecipitation-inducing activity than the 130 kDa component, when compared on the basis of equivalent myosin light chain kinase activity. In this study, we isolated a cDNA for the entire coding region of the 155 kDa protein. The deduced amino acid sequence revealed a high degree of similarity to those of chicken and rabbit smooth muscle myosin light chain kinases. Multiple motifs, such as three repeats of an immunoglobulin C2-like domain, a fibronectin type III domain, and unusual 20 repeats of 12 amino acids were detected in the sequence. Part of the amino-terminal sequence was similar to that of the actin- and calmodulin-binding domain of smooth muscle caldesmon. Them observations suggest that the 155 kDa protein has additional functions other than its enzymatic activity. Two mRNAs of 6.0 and 2.6 kb in length in the bovine stomach smooth muscle RNAs were hybridized with cDNA probes. The 2.6-kb RNA probably encodes telokin, which is the carboxyl terminus of smooth muscle myosin light chain kinase. mRNAs with identical lengths were also detected in bovine aorta.
1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.
2Present addresses: Yoshizato MorphoMatrix Projed, Research Development Corporation of Japan, Tsukuba, Ibaraki 300-26
3Department of Cell Biology and Anatomy, Cornell University Medical College, 1300 York Ave., New York, 10021, U.S.A.
4Obihiro University for Agriculture and Veterinary Medicine, Obihiro, Hokkaido 080.
5Faculty of Medicine, Kyoto University, Kyoto 606.
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