Cloning and chromosomal localization of Drosophila cDNA encoding the catalytic subunit of protein phosphatase 1α. High conservation between mammalian and insect sequences
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 1α (PP‐1α) 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 troughout 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‐1α, proves the existence of at least two transcriptionally active genes for protein phosphatase 1.
Additional Information
© FEBS 1989. (Received February 13/April 24, 1989) Thanks are due to Dr D. Kalderon and Professor G. M. Rubin for the Drosophila cDNA library and to Mr A. I. H. Murchie for the synthesis of oligonucleotides. This work was supported by a grant from the Wellcome Trust and Group Support from the Medical Research Council, London (to P. T. W. C.) and a grant from the Cancer Research Campaign (to D. M. G.). J. M. Axton held a Science and Engineering Research Council Studentship. V. Dombradi was supported by a Long-Term EMBO Fellowship and was on leave from the Institute of Medical Chemistry, University School of Medicine, Debrecen, Hungary. The novel nucleotide sequence published here has been deposited with the EMBL and GenBank sequence data banks and is available under the accession number X15583.Additional details
- Eprint ID
- 106043
- DOI
- 10.1111/j.1432-1033.1989.tb21089.x
- Resolver ID
- CaltechAUTHORS:20201013-145241560
- Wellcome Trust
- Medical Research Council (UK)
- Cancer Research Campaign
- Science and Engineering Research Council (SERC)
- European Molecular Biology Organization (EMBO)
- Created
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2020-10-13Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field