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

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 m...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-04, Vol.343 (1), p.244-251
Main Authors: Chan, Catherine S., Howell, Jenika M., Workentine, Matthew L., Turner, Raymond J.
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
AMINO ACID SEQUENCE
ARGININE
CALORIMETRY
CELL MEMBRANES
Chaperone
ENZYMES
ESCHERICHIA COLI
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Escherichia coli Proteins - physiology
FRACTIONATION
Membrane Transport Proteins - genetics
Membrane Transport Proteins - physiology
Molecular Chaperones - chemistry
Molecular Chaperones - metabolism
Molecular Sequence Data
MOLYBDENUM
NarJ
Nitrate Reductase - chemistry
Nitrate Reductase - metabolism
Nitrate reductase A
NITRATES
Protein Conformation
Protein Interaction Mapping
Redox enzyme
Redox enzyme maturation protein
TITRATION
TRANSLOCATION
Twin-arginine translocation
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2006.02.133