Williams, Mary , Smith, Melissa .
Phylogenetic analysis and functional characterization of the SAC9 protein in Arabidopsis and Chlamydomonas.
Phosphoinositides (PI) are membrane-associated phospholipids that perform a key role in intracellular signaling. The metabolism of these PIs is partly regulated by PI phosphatases including SAC domain phosphatases. SAC domain proteins have been found in a wide variety of eukaryotic species and each is characterized by a highly conserved ~500 amino acid long SAC domain. However, modifications within the SAC domain and the C-terminal region have led to different SAC domain proteins with distinct biochemical and functional properties. SAC9 proteins are the most divergent of all SAC domain proteins. SAC9 was originally only identified in Arabidopsis and rice. Recently, we have identified orthologues in alfalfa, moss, and three green algal species. We will present a phylogenetic analysis of the SAC9 protein that we are using to inform our experiments to investigate functional domains in the SAC9 protein. We will also present results from our ongoing studies of the Arabidopsis SAC9 protein including in vitro activity assays and cellular localization studies in transgenic Arabidopsis.
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1 - Harvey Mudd College, Biology Department, 301 Platt Blvd, Claremont, CA, 91711, USA
2 - Harvey Mudd College, Biology, 340 E Foothill Blvd, Claremont, CA, 91711, US
Presentation Type: Plant Biology Abstract
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM