Poster: Late and Moved Abstracts
Abs #
975: Structure-function studies of NPH3: a blue light photoreceptor interacting protein
Light is a vital environmental signal that controls many processes of growth and development in plants. Light is perceived by sensory photoreceptors that enable the plant to respond to a variety of alterations in the light environment. The previously identified NPH3 gene encodes a novel plant-specific protein that is necessary for normal phototropic response of Arabidopsis thaliana and has been shown to physically interact with phototropin 1 (phot1), a blue light receptor controlling this response. Yet little is know about how NPH3 mediates the transduction of signals from phot1. As one approach to gaining clarity on this issue we are examining NPH3 localization and how this localization may change in response to light in planta by in situ immunohistochemistry and confocal microscropy. We are also generating transgenic plants expressing a NPH3::eYFP fusion protein so that similar studies can be done in living tissues. Concomitant with these studies we will be following phot1 protein localization by similar methods using different fluorophores. As another approach to understand NPH3 function we are designing a yeast-three-hybrid screen with a phot1-NPH3 complex as a bait to identify additional components of the presumed signaling complex. Lastly we are attempting to express sufficient quantities of highly purified NPH3 for crystallization and subsequent 3-D structure studies. We see these latter studies as extremely important as the knowledge about the structure of this novel protein will be extremely informative relative to questions of function and protein-protein interactions, both with respect to known entities and development of new approaches.
