| Abstract Detail
Protein Modification and Turnover Zeng, Qin [1], Wang, Xuejun [2], Mucha, Andrew [2], Sutton, Safira [2], Running, Mark [2]. A novel protein prenyltransferase α-subunit-like gene (PPAL) is required for seedling development and fertility in Arabidopsis thaliana. Protein prenylation plays important roles in protein-membrane association and protein-protein interactions. There are three typical protein prenyltransferases in all eukaryotic organisms, protein farnesyltransferase (PFT), protein geranylgeranyltransferase I (PGGT-I), and protein geranylgeranyltransferase II or Rab geranylgeranyltransferase (Rab-GGT). PFT and PGGT-I share a common α-subunit while Rab-GGT has a distinct α-subunit. We have identified a novel Arabidopsis protein, PPAL, which has weak similarity to the known α-subunits of prenyl transferases. PPAL homologues are found in rice, mammals and certain other animals, but not in yeast. The function of PPAL homologs are unknown, and the only reported mutant, in Drosophila, is lethal. Arabidopsis ppal mutants are viable but show slower growth, with the most dramatic phenotypes in seed germination, sugar response, and fertility. In a directed yeast two-hybrid assay, PPAL interacts with one of the putative Rab-GGT β-subunits, RGTB1. When co-expressed in Saccharomyces cerevisiae, PPAL was co-purified with FLAG-tagged RGTB1, further suggesting their possible physical interaction in plants. The enzymatic function of PPAL and the degree of functional conservation of PPAL among species is currently under investigation.
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1 - Donald Danforth Plant Science Center, Running Lab, 975 N Warson Rd, St. Louis, MO, 63132, USA
2 - Donald Danforth Plant Science Center, Running Lab
Keywords:
protein prenyltransferase
protein prenylation
seed germination.
Presentation Type: Plant Biology Abstract
Session: P
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM
Number: P37001
Abstract ID:103 |
