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Molecular cloning of a 74‐kDa regulatory subunit (B″ or δ) of human protein phosphatase 2A
Author(s) -
Tanabe Osamu,
Nagase Terumasa,
Murakami Takehiko,
Nozaki Hideto,
Usui Hirofumi,
Nishito Yasumasa,
Hayashi Hideyuki,
Kagamiyama Hiroyuki,
Takeda Masao
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01500-0
Subject(s) - protein subunit , biology , complementary dna , microbiology and biotechnology , cdna library , peptide sequence , protein phosphatase 2 , gamma aminobutyric acid receptor subunit alpha 1 , open reading frame , phosphatase , interleukin 10 receptor, alpha subunit , heterotrimeric g protein , biochemistry , phosphorylation , g alpha subunit , gene , g protein , signal transduction
Based on amino acid sequence data of a 74‐kDa regulatory subunit (B″ or δ) of a human heterotrimeric protein phosphatase 2A, a cDNA encoding the subunit was isolated from a human cerebral cortex library. The cDNA had an open reading frame encoding an M r 66 138 protein of 570 amino acids. Bacterial expression of the cDNA yielded a protein immunoreactive with antisera specific to the 74‐kDa subunit. The predicted primary structure of the subunit had no similarity to already reported sequences of PP2A regulatory subunits including A, B, and PR72. Potential phosphorylation sites for protein kinases A and C, a bipartite motif of putative nuclear localization signal, an SH3 accessible proline‐rich domain, and a unique PQ repeat were found in the sequence. The subunit mRNA of about 2.9 kb was ubiquitously expressed in rat tissues.