Cloning of the cDNA encoding the myosin heavy chain of a vertebrate cellular myosin
| Autor: | Sachiyo Kawamoto, Robert S. Adelstein, Mary Anne Conti, David A. Brill, Ralph V. Shohet, Yvette A. Preston |
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| Jazyk: | angličtina |
| Rok vydání: | 1989 |
| Předmět: |
animal structures
Molecular Sequence Data Restriction Mapping Biology Major histocompatibility complex Epithelium Complementary DNA Sequence Homology Nucleic Acid Myosin Animals Humans Amino Acid Sequence Binding site Cloning Molecular Peptide sequence Gene Library Cloning chemistry.chemical_classification Multidisciplinary Base Sequence Protein primary structure Myosin Subfragments Nucleic Acid Hybridization DNA Blotting Northern Molecular biology Amino acid chemistry Organ Specificity biology.protein Chickens Research Article |
| Zdroj: | Scopus-Elsevier |
| Popis: | 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 alpha-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. |
| Databáze: | OpenAIRE |
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