Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870628 | FEBS Letters | 2014 | 8 Pages |
Abstract
14-3-3 Proteins bind phosphorylated sequences in proteins and regulate multiple cellular functions. For the first time, we show that pure recombinant human 14-3-3 ζ, γ, ε and Ï isofoms hydrolyze ATP with similar Km and kcat values. In sharp contrast the sigma isoform has no detectable activity. Docking studies identify two putative binding pockets in 14-3-3 zeta. Mutation of D124A in the amphipathic pocket enhances binding affinity and catalysis. Mutation of a critical Arg (R55A) at the dimer interface in zeta reduces binding and decreases catalysis. These experimental results coincide with a binding pose at the dimer interface. This newly identified function could be a moon lighting function in some of these isoforms.
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Authors
Manoj P. Ramteke, Pradnya Shelke, Vidhya Ramamoorthy, Arun Kumar Somavarapu, Amit Kumar Singh Gautam, Padma P. Nanaware, Sudheer Karanam, Sami Mukhopadhyay, Prasanna Venkatraman,