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PMID: 2550221 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Cloning and chromosomal localization of Drosophila cDNA encoding the catalytic subunit of protein phosphatase 1 alpha. High conservation between mammalian and insect sequences.

European journal of biochemistry ·Vol. 183 ·No. 3 ·1989-08-15 ·Pages 603-10

Dombrádi V, Axton JM, Glover DM, Cohen PT

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Biological Evolution Chromosome Mapping Cloning, Molecular DNA/genetics Drosophila melanogaster/enzymology,genetics Genes Macromolecular Substances Molecular Sequence Data Oligonucleotide Probes Phosphoprotein Phosphatases/genetics Protein Biosynthesis Protein Phosphatase 1 Rabbits/genetics Salivary Glands/enzymology Sequence Homology, Nucleic Acid X Chromosome
Chemicals
Macromolecular Substances Oligonucleotide Probes DNA Phosphoprotein Phosphatases Protein Phosphatase 1
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Dombrádi V
Department of Biochemistry, Medical Sciences Institute, The University, Dundee, Scotland.
Axton J M
Glover D M
Cohen P T
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1989-08-15
Pages
603-10
Language
English
Region
England
NLM ID
0107600
Subset
IM
Grants
Wellcome Trust · United Kingdom
Databases
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