A 3.5 kb cDNA clone was isolated from bovine adrenal gland cDNA library. The clone contained a full-length 3.1 kb open reading frame, encoding a novel myosin I. The deduced amino acid sequence was highly homologous to other known myosin Is in the N-terminal 2 kb region which corresponds to the myosin head domain, while no strong homology was detected in the tail region. The head-tail junction contained the Ca(2+)-independent calmodulin binding consensus sequence, suggesting that the novel myosin I binds calmodulin. This was confirmed by calmodulin overlay which showed the binding of 125I-calmodulin to the recombinant myosin I expressed in E. coli. Northern blots with probes from head and tail regions of this myosin I revealed that this novel myosin I is widely distributed among various tissues.
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Zhu et al. (1994) studied this question.
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