cDNA cloning of a novel B subunit of Xenopus protein phosphatase 2A and its biological activity in oocytes

Biochem Biophys Res Commun. 1997 Mar 6;232(1):218-22. doi: 10.1006/bbrc.1997.6259.

Abstract

We have cloned a cDNA encoding a novel B regulatory subunit of protein phosphatase 2A (PP2A) from a Xenopus oocyte cDNA library. The novel B subunit, termed B beta', shows the strongest overall sequence similarity to, but a distinct N-terminal sequence from, the beta isoform of the human/rat B subunit. When expressed ectopically in Xenopus oocytes, the B beta' isoform can augment the endogenous PP2A activity and inhibit oocyte maturation induced by progesterone. These results suggest that the B beta' isoform can form a complex with other PP2A subunits to make a trimeric PP2A holoenzyme in Xenopus oocytes and may negatively control the initiation of oocyte maturation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • Molecular Sequence Data
  • Oocytes / enzymology*
  • Phosphoprotein Phosphatases / chemistry
  • Phosphoprotein Phosphatases / genetics*
  • Protein Phosphatase 2
  • Rats
  • Sequence Homology, Amino Acid
  • Xenopus

Substances

  • DNA, Complementary
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 2

Associated data

  • GENBANK/AB000406