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Sequences determining the cytoplasmic localization of a chemoreceptor domain
L Seligman1, J Bailey, C Manoil
1Department of Genetics, University of Washington, Seattle 98195, USA.
Journal of Bacteriology
|May 1, 1995
Summary
The Escherichia coli serine chemoreceptor (Tsr) protein
Area of Science:
- Molecular Biology
- Protein Structure
- Cell Biology
Background:
- The Escherichia coli serine chemoreceptor (Tsr) exhibits a specific membrane topology.
- Understanding protein topology is crucial for cellular function.
Purpose of the Study:
- To investigate sequence elements governing the C-terminal domain localization of the Tsr protein.
- To elucidate the mechanisms of Tsr membrane topology generation.
Main Methods:
- Utilized chemoreceptor-alkaline phosphatase gene fusions to analyze Tsr protein localization.
- Introduced mutations and deletions in Tsr sequence elements.
Main Results:
- C-terminal domain localization depends on the TM2 segment and tolerates charge mutations.
- Wild-type periplasmic domain size influences C-terminal domain export, suggesting partial membrane misinsertion.
- Single transmembrane segments (TM1 or TM2) insertion is regulated by adjacent charged or amphipathic sequences.
Conclusions:
- Tsr membrane topology generation is an overdetermined process.
- An interplay of sequences promotes and opposes the establishment of normal Tsr structure.