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A novel myosin I from bovine adrenal gland
Author(s) -
Zhu Tong,
Ikebe Mitsuo
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80378-1
Subject(s) - myosin , calmodulin , myosin light chain kinase , complementary dna , microbiology and biotechnology , biology , peptide sequence , open reading frame , cdna library , biochemistry , gene , enzyme
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 headtail 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 125 I‐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.