Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11
| Autor: | A H, Beggs, T J, Byers, J H, Knoll, F M, Boyce, G A, Bruns, L M, Kunkel |
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| Rok vydání: | 1992 |
| Předmět: |
Base Sequence
Transcription Genetic Chromosomes Human Pair 11 Muscles Molecular Sequence Data Chromosome Mapping Spectrin DNA Hybrid Cells Blotting Northern Polymerase Chain Reaction Fluorescence Dystrophin Chromosomes Human Pair 1 RNA Ribosomal Sequence Homology Nucleic Acid Humans Actinin Amino Acid Sequence Cloning Molecular Sequence Alignment |
| Zdroj: | The Journal of biological chemistry. 267(13) |
| ISSN: | 0021-9258 |
| Popis: | Conserved sequences of dystrophin, beta-spectrin, and alpha-actinin were used to plan a set of degenerate oligonucleotide primers with which we amplified a portion of a human alpha-actinin gene transcript. Using this short clone as a probe, we isolated and characterized full-length cDNA clones for two human alpha-actinin genes (ACTN2 and ACTN3). These genes encode proteins that are structurally similar to known alpha-actinins with approximately 80% amino acid identity to each other and to the previously characterized human nonmuscle gene. ACTN2 is the human homolog of a previously characterized chicken gene while ACTN3 represents a novel gene product. Northern blot analysis demonstrated that ACTN2 is expressed in both skeletal and cardiac muscle, but ACTN3 expression is limited to skeletal muscle. As with other muscle-specific isoforms, the EF-hand domains in ACTN2 and ACTN3 are predicted to be incapable of binding calcium, suggesting that actin binding is not calcium sensitive. ACTN2 was mapped to human chromosome 1q42-q43 and ACTN3 to 11q13-q14 by somatic cell hybrid panels and fluorescent in situ hybridization. These results demonstrate that some of the isoform diversity of alpha-actinins is the result of transcription from different genetic loci. |
| Databáze: | OpenAIRE |
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