Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

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

This Article
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow All Versions of this Article:
140/2/647    most recent
pp.105.073916v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sehnke, P. C
Right arrow Articles by Ferl, R. J
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sehnke, P. C
Right arrow Articles by Ferl, R. J
Agricola
Right arrow Articles by Sehnke, P. C
Right arrow Articles by Ferl, R. J

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.




This article has been cited by other articles:


Home page
 Plant Physiol.Home page
J. D. Mayfield, K. M. Folta, A.-L. Paul, and R. J. Ferl
The 14-3-3 Proteins {micro} and {upsilon} Influence Transition to Flowering and Early Phytochrome Response
Plant Physiology, December 1, 2007; 145(4): 1692 - 1702.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 2006 by the American Society of Plant Biologists