2004 Student Research Conference:
17th Annual Student Research Conference


atDjB48, a Previously Uncharacterized Molecular Chaperone from Arabidopsis thaliana
William G. Alexander
Dr. Cynthia Cooper, Faculty Mentor

DnaJ was originally isolated from E. coli as a heat shock protein. It was found to form a molecular chaperone machine by combining with DnaK and GrpE. DnaJ contains a 75 a. a. domain, called the J-domain, which is centered around a HPD tripeptide. This peptide is essential for molecular chaperone action, and is found in all chaperones. A. thaliana has many of these J-domain proteins, most of which have not been characterized save for sequencing. A. thaliana RNA was extracted from four tissues, reverse-PCR technique was used to amplify the gene for chaperone protein atDjB48, and the cDNA was sequenced.The sequence obtained matched perfectly with the predicted sequence from the annotated A. thaliana genome. Vectors for atDjB48 expression in E. coli are currently being constructed.

Keywords: A. thaliana, chaperone, heat shock protein, J-domain, HPD tripeptide, atDjB48, DnaJ, Hsp70


Presentation Type: Poster

Session: 26-35
Location: OP Lobby & Atrium
Time: 1:15

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