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Title: Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli

Abstract

NarJ is a chaperone involved in folding, maturation, and molybdenum cofactor insertion of nitrate reductase A from Escherichia coli. It has also been shown that NarJ exhibits sequence homology to a family of chaperones involved in maturation and cofactor insertion of E. coli redox enzymes that are mediated by twin-arginine translocase (Tat) dependent translocation. In this study, we show that NarJ binds the N-terminal region of NarG through Far Western studies and isothermal titration calorimetry, and the binding event occurs towards a short peptide sequence that contains a homologous twin-arginine motif. Fractionation experiments also show that the interaction of NarJ to the cytoplasmic membrane exhibits Tat-dependence. Upon further investigation through Far Western blots, the interactome of NarJ also exhibits Tat-dependence. Together the data suggest that the Tat system may play a role in the maturation pathway of nitrate reductase A.

Authors:
 [1];  [1];  [1];  [2]
  1. Department of Biological Science, BI 156 Biological Sciences Bldg, University of Calgary, 2500 University Dr NW, Calgary, Alta., T2N 1N4 (Canada)
  2. Department of Biological Science, BI 156 Biological Sciences Bldg, University of Calgary, 2500 University Dr NW, Calgary, Alta., T2N 1N4 (Canada). E-mail: turnerr@ucalgary.ca
Publication Date:
OSTI Identifier:
20798925
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 343; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2006.02.133; PII: S0006-291X(06)00403-7; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AMINO ACID SEQUENCE; ARGININE; CALORIMETRY; CELL MEMBRANES; ENZYMES; ESCHERICHIA COLI; FRACTIONATION; MOLYBDENUM; NITRATES; TITRATION; TRANSLOCATION

Citation Formats

Chan, Catherine S., Howell, Jenika M., Workentine, Matthew L., and Turner, Raymond J. Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli. United States: N. p., 2006. Web. doi:10.1016/j.bbrc.2006.02.133.
Chan, Catherine S., Howell, Jenika M., Workentine, Matthew L., & Turner, Raymond J. Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli. United States. doi:10.1016/j.bbrc.2006.02.133.
Chan, Catherine S., Howell, Jenika M., Workentine, Matthew L., and Turner, Raymond J. Fri . "Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli". United States. doi:10.1016/j.bbrc.2006.02.133.
@article{osti_20798925,
title = {Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli},
author = {Chan, Catherine S. and Howell, Jenika M. and Workentine, Matthew L. and Turner, Raymond J.},
abstractNote = {NarJ is a chaperone involved in folding, maturation, and molybdenum cofactor insertion of nitrate reductase A from Escherichia coli. It has also been shown that NarJ exhibits sequence homology to a family of chaperones involved in maturation and cofactor insertion of E. coli redox enzymes that are mediated by twin-arginine translocase (Tat) dependent translocation. In this study, we show that NarJ binds the N-terminal region of NarG through Far Western studies and isothermal titration calorimetry, and the binding event occurs towards a short peptide sequence that contains a homologous twin-arginine motif. Fractionation experiments also show that the interaction of NarJ to the cytoplasmic membrane exhibits Tat-dependence. Upon further investigation through Far Western blots, the interactome of NarJ also exhibits Tat-dependence. Together the data suggest that the Tat system may play a role in the maturation pathway of nitrate reductase A.},
doi = {10.1016/j.bbrc.2006.02.133},
journal = {Biochemical and Biophysical Research Communications},
number = 1,
volume = 343,
place = {United States},
year = {Fri Apr 28 00:00:00 EDT 2006},
month = {Fri Apr 28 00:00:00 EDT 2006}
}