Cloning and chromosomal localization of Drosophila cDNA encoding the catalytic subunit of protein phosphatase 1 alpha. High conservation between mammalian and insect sequences
| Autor: | J.Myles Axton, David M. Glover, Patricia T.W. Cohen, Viktor Dombrádi |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
X Chromosome
Macromolecular Substances Protein subunit Phosphatase Molecular Sequence Data Biology Biochemistry Salivary Glands Complementary DNA Protein Phosphatase 1 Sequence Homology Nucleic Acid Phosphoprotein Phosphatases Animals Amino Acid Sequence Cloning Molecular Polytene chromosome Base Sequence cDNA library Nucleic acid sequence Chromosome Mapping Protein phosphatase 1 DNA Molecular biology Biological Evolution Drosophila melanogaster Chromosome 3 Genes Protein Biosynthesis Rabbits Oligonucleotide Probes |
| Zdroj: | European journal of biochemistry. 183(3) |
| ISSN: | 0014-2956 |
| Popis: | A 1.2-kb clone containing the full coding sequence of a protein phosphatase 1 catalytic subunit has been isolated from a Drosophila head cDNA library. It encodes a polypeptide of 302 amino acids with a molecular mass of 34.5 kDa. The predicted protein sequence is 92% identical (94% similar) to rabbit protein phosphatase 1 alpha (PP-1 alpha) demonstrating strict conservation of the phosphatase catalytic subunit over a considerable evolutionary distance. Abundant 1.6-kb and 2.5-kb mRNA transcripts were detected throughout Drosophila development. The clone hybridised to four sites on Drosophila salivary gland polytene chromosomes. The major site is at 87B6-12 on the right arm of chromosome 3. In addition, there are three secondary sites, one on the same chromosome at 96A2-5 and two on the X chromosome at 9C1-2 and 13C1-2. Isolation of a further cDNA clone, hybridising to 9C1-2 and encoding part of the catalytic subunit 88% similar to Drosophila PP-1 alpha, proves the existence of at least two transcriptionally active genes for protein phosphatase 1. |
| Databáze: | OpenAIRE |
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