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Published on January 11, 2006; 10.1104/pp.105.073916

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Received November 7, 2005
Returned for revision December 6, 2005
Accepted December 6, 2005

Exposed loop Domains of Complexed 14-3-3 Proteins Contribute to Structural Diversity and Functional Specificity

Paul C Sehnke , Beth Laughner , Helene Cardasis , David Powell , and Robert J Ferl *

Program in Plant Molecular and Cellular Biology, Department of Horticultural Science, University of Florida, Gainesville, Florida, 32611
Department of Chemistry, University of Florida, Gainesville, Florida, 32611

* Corresponding author; email: robferl{at}ufl.edu.

The 14-3-3 family of proteins function through protein:phosphoprotein interactions, the nature of which has been elucidated using x-ray crystallography. However, some key structural features in non-conserved regions have yet to be fully resolved, leaving open questions regarding the functional selectivity of 14-3-3 family members for diverse clients. In an effort to study surface accessible structural features in 14-3-3 containing macromolecular complexes, and to illuminate important structure / function variations among the 14-3-3 isoforms, we determined the epitopes for three unique monoclonal antibodies (mAbs) developed against the Arabidopsis thaliana G-box DNA:protein complex (GBC). The epitopes mapped to different loops in a phylogenetically important subset of the thirteen 14-3-3 family members. All three epitopes were on a common exposed face of complexed 14-3-3s. Two of the mAbs recognized linear sequences within loops 5 and 6, while the third mAb recognized 14-3-3 residues surrounding the pivotal medial glycine (Gly) in the divalent cation binding domain of loop 8, together with distal residue(s) in the putative dynamic tenth helix that has yet to be determined by crystallography. Gly at this loop 8 position is unique to non epsilon 14-3-3 isoforms of the plant kingdom, suggesting that this region constitutes a plant specific key functional 14-3-3 feature and highlighting that the loop 8 region is functionally significant. Mutagenesis of the medial amino acid in the loop 8 domain changed the flexibility of the C-terminus and altered client peptide binding selectivity, demonstrating the functional significance of the surface accessible, evolutionarily distinct loop 8 domain.




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