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Journal of Biochemistry 2005 138(3):245-253; doi:10.1093/jb/mvi122
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© 2005 The Japanese Biochemical Society

Regular Paper

Asymmetric Photocross-Linking of Singly Phosphorylated Smooth Muscle Heavy Meromyosin

Kosuke Takeya1, Masayuki Takahashi1, Tsuyoshi Katoh2 and Michio Yazawa1,*

1 Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810; and 2 Department of Biochemistry, Asahikawa Medical College, Asahikawa 078-8510

* To whom correspondence should be addressed. Tel: +81-11-706-3813, Fax: +81-11-706-4924, E-mail: myazawa{at}sci.hokudai.ac.jp

Although activities of smooth muscle myosin are regulated by phosphorylation, the molecular mechanisms of regulation have not been fully established. Phosphorylation of both heads of myosin is known to activate ATPase and motor activities, but the effects of phosphorylation of only one of the heads have not been established. Such information on singly phosphorylated myosin can serve to elucidate the molecular mechanism of the phosphorylation-dependent regulation. To understand the structural properties of the singly phosphorylated state, we prepared singly phosphorylated heavy meromyosin (HMM) containing a photoreactive benzophenone-labeled RLC and examined its photocross-linking reactivity. The two heads in the singly phosphorylated HMM showed different reactivities. The dephosphorylated RLC in the singly phosphorylated HMM was cross-linked to a heavy chain, like that in the dephosphorylated HMM, whereas the phosphorylated RLC did not react, like that in the fully phosphorylated HMM. These results indicate that the two heads of the singly phosphorylated HMM have an asymmetric structure, suggesting that phosphorylation of one head can to some extent activate smooth muscle HMM.


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