Isolation and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster casein kinase II
| Autor: | C. V. C. Glover, Ramesh Padmanabha, A. Saxena |
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| Rok vydání: | 1987 |
| Předmět: |
Macromolecular Substances
Recombinant Fusion Proteins Protein subunit Molecular Sequence Data Biology Complementary DNA Casein kinase 2 alpha 1 Animals Amino Acid Sequence Cloning Molecular Protein kinase A Molecular Biology Peptide sequence Immunosorbent Techniques Base Sequence Nucleic acid sequence DNA Cell Biology Molecular biology Drosophila melanogaster Genes Casein kinase 2 Casein kinases Casein Kinases Protein Kinases Research Article |
| Zdroj: | Molecular and Cellular Biology. 7:3409-3417 |
| ISSN: | 1098-5549 0270-7306 |
| DOI: | 10.1128/mcb.7.10.3409 |
| Popis: | Cloned cDNAs encoding both subunits of Drosophila melanogaster casein kinase II have been isolated by immunological screening of lambda gt11 expression libraries, and the complete amino acid sequence of both polypeptides has been deduced by DNA sequencing. The alpha cDNA contained an open reading frame of 336 amino acid residues, yielding a predicted molecular weight for the alpha polypeptide of 39,833. The alpha sequence contained the expected semi-invariant residues present in the catalytic domain of previously sequenced protein kinases, confirming that it is the catalytic subunit of the enzyme. Pairwise homology comparisons between the alpha sequence and the sequences of a variety of vertebrate protein kinase suggested that casein kinase II is a distantly related member of the protein kinase family. The beta subunit was derived from an open reading frame of 215 amino acid residues and was predicted to have a molecular weight of 24,700. The beta subunit exhibited no extensive homology to other proteins whose sequences are currently known. |
| Databáze: | OpenAIRE |
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