cDNA Cloning and Expression of the Human Homolog of the Sea UrchinfascinandDrosophila singedGenes Which Encodes an Actin-Bundling Protein
| Autor: | Michael I. Lerman, Fumio Matsumura, W. Marston Linehan, James R. Gnarra, Thomas Stackhouse, Fuh-Mei Duh, Laura Geil, Yongkai Weng, D. Roxanne Duan, Farida Latif, William S. Modi |
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| Rok vydání: | 1994 |
| Předmět: |
DNA
Complementary Molecular Sequence Data Biology Complementary DNA Genetics Animals Humans Amino Acid Sequence Lymphocytes Cloning Molecular Molecular Biology Gene Fascin Messenger RNA Base Sequence Sequence Homology Amino Acid Molecular mass cDNA library Microfilament Proteins Cell Biology General Medicine Molecular biology Fusion protein Cell culture Insect Hormones Sea Urchins biology.protein Drosophila Carrier Proteins HeLa Cells |
| Zdroj: | DNA and Cell Biology. 13:821-827 |
| ISSN: | 1557-7430 1044-5498 |
| DOI: | 10.1089/dna.1994.13.821 |
| Popis: | cDNA clones having extensive sequence identity with the sea urchin fascin and the Drosophila singed gene products were isolated from a human teratocarcinoma cDNA library. The human homolog, termed hsn, is a single-copy gene that was localized to human chromosome 7p22 by fluorescence in situ hybridization and is predicted to encode a 493-amino-acid product with a molecular mass of approximately 55,000. This protein would be similar in size to the fascin and singed proteins, as well as a previously described 55-kD actin-bundling protein that was purified from HeLa cells. Monoclonal antibodies directed against the 55-kD HeLa protein were reactive against a bacterially expressed hsn fusion protein, indicating that the hsn gene probably encodes the 55-kD protein. The hsn mRNA was variably expressed in all human tissues analyzed and was highly expressed in actively growing renal carcinoma cell lines and in activated, but not in resting, lymphocytes, suggesting a functional role for hsn in proliferation. The fascin family lacks homology with other characterized actin-binding proteins, and the high degree of evolutionary conservation of these proteins indicates a functional importance of their actin-bundling properties. |
| Databáze: | OpenAIRE |
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