Genetic Characterization of a Brain-Specific Form of the Type I Regulatory Subunit of cAMP-Dependent Protein Kinase

An isoform (RIβ ) of the regulatory type I subunit gene of cAMP-dependent protein kinase (EC 2.7.1.37) has been characterized in mouse. The open reading frame of the RIβ cDNA is 72% identical in nucleotide sequence with the previously cloned RI gene, now referred to as RIα . Both genes code for a pr...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-06, Vol.85 (11), p.3703-3707
Main Authors: Clegg, Christopher H., Cadd, Gary G., McKnight, G. Stanley
Format: Article
Language:English
Subjects:
3T3 cells
Amino Acid Sequence
Amino acids
Animals
Base Sequence
Brain - enzymology
Complementary DNA
Enzymes
Gin
Male
Messenger RNA
Mice
Molecular Sequence Data
Molecular Weight
Open reading frames
Protein Kinases - genetics
Proteins
Receptors, Cyclic AMP - genetics
RNA
RNA, Messenger - genetics
Testes
Testis - enzymology
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Summary:An isoform (RIβ ) of the regulatory type I subunit gene of cAMP-dependent protein kinase (EC 2.7.1.37) has been characterized in mouse. The open reading frame of the RIβ cDNA is 72% identical in nucleotide sequence with the previously cloned RI gene, now referred to as RIα . Both genes code for a protein of 380 amino acids and their proteins are 82% identical in amino acid sequence. Sequence similarity is highest in the regions that form the pseudosubstrate-binding site of the catalytic subunit and the two cAMP binding domains. The amino-terminal portion shows the greatest dissimilarity, suggesting that the isoforms may differ in their dimerization properties or interaction with other proteins. In contrast to RIα , which is constitutively expressed in all tissues, RIβ is expressed in a highly tissue-specific manner. Brain and spinal cord contained significant levels of RIβ mRNA, testis RNA gave a detectable signal, and all other tissues tested were negative. Expression of a RIβ cDNA in NIH 3T3 cells resulted in the appearance of a RI subunit protein that migrated more slowly than RIα after NaDodSO4/PAGE. The native form of RIβ in brain could also be distinguished from RIα by its abnormal migration on NaDodSO4/PAGE. RIβ protein produced in 3T3 cells was shown to be functional by its ability to form a cAMP-dependent holoenzyme with the catalytic subunit.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.11.3703