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Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)
Raymond J Turner1, Andriyka L Papish, Frank Sargent
1Department of Biological Sciences, University of Calgary, Alberta, Canada. turnerr@ucalgary.edu
Canadian Journal of Microbiology
|June 24, 2004
Summary
The twin-arginine protein transport (Tat) system exports folded proteins. This study reveals an unexpected evolutionary link between Tat accessory proteins and cofactor insertion, specifically DmsD and NarJ in E. coli.
Area of Science:
- Molecular biology
- Protein transport
- Biochemistry
Background:
- The twin-arginine protein transport (Tat) system exports folded proteins across membranes.
- Cofactor insertion occurs before Tat transport, necessitating regulation to prevent immature substrate export.
Purpose of the Study:
- To investigate primary sequence relationships between accessory proteins involved in Tat substrate maturation.
- To understand regulatory mechanisms preventing premature or competitive export of Tat substrates.
Main Methods:
- Comparative analysis of primary sequences of accessory proteins.
- Identification of redox enzyme maturation proteins (REMPs) linked to Tat transport.
- Focus on respiratory enzyme assembly in Escherichia coli.
Main Results:
- Assignment of a REMP for each studied respiratory enzyme.
- Discovery of a significant, previously unrecognized link between DmsD (Tat-linked REMP) and NarJ (nitrate reductase biosynthetic protein).
Conclusions:
- The findings suggest an evolutionary connection between Tat transport and cofactor insertion processes.
- This link may play a role in regulating the assembly of complex respiratory enzymes.