Characterization of the Binding Interaction between the Oncoprotein Gankyrin and a Grafted S6 ATPase
Author(s) -
Alex M. Chapman,
Bryce E. Rogers,
Brian R. McNaughton
Publication year - 2014
Publication title -
biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.43
H-Index - 253
eISSN - 1520-4995
pISSN - 0006-2960
DOI - 10.1021/bi5012354
Subject(s) - isothermal titration calorimetry , atpase , recombinant dna , protein subunit , escherichia coli , chemistry , biochemistry , aaa proteins , binding site , plasma protein binding , microbiology and biotechnology , biophysics , biology , enzyme , gene
A complex with the C-terminal portion of the proteosomal subunit S6 ATPase is the only available structure of a protein-protein interaction involving the oncoprotein gankyrin. However, difficulties associated with recombinant expression of S6 ATPase alone, or truncations thereof, have limited our understanding of this assembly. We replaced the C-terminal portion of FtsH from Escherichia coli with the structurally homologous C-terminal portion of S6 ATPase and used this grafted protein to characterize the gankyrin-S6 ATPase binding interaction by isothermal titration calorimetry.
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