Cloning of the cDNA Encoding the Myosin Heavy Chain of a Vertebrate Cellular Myosin

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 86; no. 20; pp. 7726 - 7730
• Main Authors: Shohet, Ralph V., Conti, Mary Anne, Kawamoto, Sachiyo, Preston, Yvette A., Brill, David A., Adelstein, Robert S.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 01.10.1989; National Acad Sciences
• Subjects: Amino Acid Sequence; Amino acids; Animals; Base Sequence; Blotting, Northern; Chickens; Cloning, Molecular; Complementary DNA; DNA - genetics; Epithelial cells; Epithelium - metabolism; Gene Library; genes; Humans; intestine; Libraries; Messenger RNA; Molecular Sequence Data; Myosin Subfragments - genetics; Nucleic Acid Hybridization; Nucleotides; Organ Specificity; Restriction Mapping; RNA; Sequence Homology, Nucleic Acid; Smooth muscle; Vertebrates
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.86.20.7726

The complete amino acid sequence of a vertebrate cellular myosin heavy chain (MHC; 1,959 amino acids, 226 kDa) has been deduced by using cDNA clones from a chicken intestinal epithelial cell library. RNA blot analysis of kidney, spleen, brain, liver, and intestinal epithelial cells as well as smooth muscle cells from the aorta and gizzard indicates the presence of a 7.3-kilobase (kb) message that is larger than the message for chicken smooth and striated muscle MHC. The chicken intestinal epithelial cell MHC shows overall similarity in primary structure to other MHCs in the areas of the reactive thiol residues and in areas contributing to the ATP binding site and actin binding site. The globular head domain is followed by an α -helical coiled-coil region, and as in smooth muscle MHC there is a short uncoiled sequence at the carboxyl terminus of the molecule. Comparison of amino acid sequences in the rod regions between human and chicken cellular MHCs shows a remarkable 92% identity.