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Title: Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions
Authors: Marcus, Nancy Y ×
Marcus, Roland A
Schmidt, Bela
Haslam, David B #
Issue Date: Dec-2007
Publisher: Academic Press
Series Title: Archives of Biochemistry and Biophysics vol:468 issue:2 pages:147-158
Abstract: Cytoplasmic type 1 DnaJ/Hsp40 chaperones contain a Cys-rich domain consisting of four CXXCXG motifs that are in a reduced state and coordinate zinc, stabilizing the intervening sequence in a loop structure. However, the Cys-rich region of the endoplasmic reticulum localized HEDJ (ERdj3/ERj3p), is considerably different in sequence and arrangement. Unlike the typical type I molecule, the HEDJ CXC, and CXXC motifs were demonstrated in this study to be predominantly oxidized in intramolecular disulfide bonds. In the native state, HEDJ bound to immobilized, denatured thyroglobulin. Unlike its binding partner GRP78, redox conditions affected the interaction of HEDJ with substrate. Substitution of the Cys-rich domain cysteine residues with serine diminished or abolished HEDJ binding in the in vitro assay. These findings suggest that the Cys-rich region of HEDJ and its oxidation state are important in maintaining the substrate interaction domain in a binding-competent conformation. (c) 2007 Elsevier Inc. All rights reserved.
URI: 
ISSN: 0003-9861
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

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