Mutations in the autoinhibitor site of the regulatory subunit of cAMP-dependent protein kinase I. Replacement of Ala-97 and Ser-99 interferes with reassociation with the catalytic subunit.

Abstract excerpt

Each regulatory (R) subunit of cAMP-dependent protein kinase contains an autoinhibitor site that lies approximately 90-100 residues from the amino terminus. In order to study the importance of this autoinhibitor site in the type I R-subunit for interacting with the catalytic (C) subunit, recombinant techniques were used to replace Ala-97 with Gln, His, Lys, and Arg and to replace Ser-99 with Gly and Lys. All of...

Topics

• Adenosine Triphosphate
• Amino Acid Sequence
• Cyclic AMP
• DNA
• Electrophoresis, Polyacrylamide Gel
• Hydrogen-Ion Concentration
• Molecular Sequence Data
• Mutagenesis, Site-Directed
• Mutation
• Phosphorylation