Record Details

N-Terminal His-Tagged AtTPR7 Interactions with Hsp70 and Hsp90 Proteins

Scientific Journals of Bogor Agricultural University

View Archive Info
 
 
Field Value
 
Title N-Terminal His-Tagged AtTPR7 Interactions with Hsp70 and Hsp90 Proteins
 
Creator PRADITA, ANANDAYU
SCHWEIGER, REGINA
SCHWENKERT, SERENA
SOLL, J√úRGEN
 
Subject AtTPR7; Chaperones; Hsp90; Hsp70; Pull down assay
 
Description Post-translational protein import into organelles is an important process to maintain cellular functions. During preprotein transport in the cytosol, chaperones, such as heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90), are functioning to prevent aggregation and to maintain the correct protein folding of preproteins. This research was conducted in order to understand the chaperone-mediated, post-translational import of preproteins into the endoplasmic reticulum of Arabidopsis thaliana. AtTPR7 (Arabidopsis thaliana Tetratrico Peptide Repeat 7) is found in the endoplasmic reticulum and contains TPR domain, which mediates protein interaction with cytosolic Hsp70 and Hsp90. In this study, recombinant AtTPR7 was expressed in E. coli BL21 (DE3)-RIPL cells and purified using an N-terminal His-tag. In order to study the interactions of the protein with the chaperones, we used pulldown and Western blot assays. We could thereby show that the N-terminally His-tagged AtTPR7 protein interacted with Hsp70 and Hsp90.
 
Publisher Bogor Agricultural University, Indonesia
 
Contributor
 
Date 2014-12-01
 
Type info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion

 
Format application/pdf
 
Identifier http://journal.ipb.ac.id/index.php/hayati/article/view/8984
 
Source HAYATI Journal of Biosciences; Vol 21, No 4 (2014): December 2014; 197-200
2086-4094
1978-3019
 
Language eng
 
Relation http://journal.ipb.ac.id/index.php/hayati/article/view/8984/7034