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Abstract Detail


Organelle Biology

Ray, Elizabeth A. [1], Bartel, Bonnie [2].

Searching for new peroxins in Arabidopsis.

Peroxisomes carry out diverse functions in Arabidopsis, including fatty acid β-oxidation, hydrogen peroxide decomposition, and conversion of indole-3-butyric acid (IBA) to indole-3-acetic acid (IAA). These single membrane bound organelles contain no DNA, and so all peroxisomal matrix proteins must be imported post-translationally. The proteins responsible for matrix protein import are known as peroxins. Peroxins in yeast have been identified through genetic screens and human homologs for many of these are the genes defective in peroxisome biogenesis disorders. Although many proteins have been identified that play a role in matrix protein import, the process is still incompletely understood, and not all proteins involved in matrix protein import in yeast and mammals have identified homologs in Arabidopsis. For example, the peroxin that tethers PEX6 to the peroxisome membrane, Pex15p in yeast and PEX26 in humans, is not apparent in the Arabidopsis genome. We hypothesize that components of the receptor recycling machinery that are conserved between yeast and mammals also have homologs in Arabidopsis. We are combining bioinformatic and functional yeast expression approaches to identify PEX15/26 candidates in Arabidopsis, and will characterize the roles of these candidates in peroxisomal function.


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1 - Rice University, Biochemistry and Cell Biology, 6100 Main St, Houston, TX, 77005, USA
2 - Rice University, Biochemistry and Cell Biology

Keywords:
none specified

Presentation Type: Plant Biology Abstract
Session: P
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM
Number: P18024
Abstract ID:1446


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