Isolation and sequence analysis of a cDNA clone encoding a type-1 protein phosphatase catalytic subunit: Homology with protein phosphatase 2A

Norbert Berndt, David G. Campbell, F. Barry Caudwell, Philip Cohen, Edgar F. da Cruz e Silva, Odete B. da Cruz e Silva, Patricia T.W. Cohen

Research output: Contribution to journalArticlepeer-review

113 Citations (Scopus)

Abstract

A 1.5 kb clone containing the full-length coding sequence of a type-1 protein phosphatase catalytic subunit has been isolated from a rabbit skeletal muscle cDNA library constructed in λgt10. The protein sequence deduced from the cDNA contains 311 residues and has a molecular mass of 35.4 kDa. A single mRNA species at 1.6 kb was visualized by Northern blotting. The type-1 protein phosphatase was strikingly homologous to protein phosphatase 2A, 49% of the amino acids between residues 11 and 280 being identical. The first 10 and last 31 residues were dissimilar. Residues 1-101 of the type-1 protein phosphatase also showed 21% sequence identity with a region of mammalian alkaline phosphatases.

Original languageEnglish
Pages (from-to)340-346
Number of pages7
JournalFEBS Letters
Volume223
Issue number2
DOIs
Publication statusPublished - 2 Nov 1987

Keywords

  • Amino acid sequence homology
  • cDNA cloning
  • Nucleotide sequence
  • Protein phosphatase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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