|Suo, Y - UNIV OF MISSOURI|
Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: August 3, 2002
Publication Date: N/A
Technical Abstract: The genome of the model plant Arabidopsis thaliana encodes an unexpectedly large number of J-domain chaperone proteins. There are a total of 90 genes, and the proteins have been assigned to 51 families (Miernyk 2001 Cell Stress Chap 6: 209-218). Family 4 consists of atDjC6 and atDjB37. These proteins do not have closely related orthologs in microbial or mammalian cells. We have previously established that atDjC6 is nuclear localized. We now report that atDjB37 is also a nuclear protein. The atDjB37-GFP chimera was transiently expressed in tobacco BY-2 cells, and localized by laser confocal microscopy. These results raise the question; why are there two chaperone proteins that have closely related primary sequences and are localized within the same subcellular compartment? As a first step towards trying to answer this question, we are using a ribonuclease protection assay to simultaneously measure mRNA expression. Results will be presented from different developmental stages, plant organs, and physiological conditions.