Journal
GENERAL PHYSIOLOGY AND BIOPHYSICS
Volume 30, Issue 3, Pages 286-292Publisher
GENERAL PHYSIOL AND BIOPHYSICS
DOI: 10.4149/gpb_2011_03_286
Keywords
Tellurite resistance; Amphitropic protein; Cross-linking; TerB protein
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Funding
- APVV [20-054005]
- VEGA [1/0346/10]
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The tellurite resistance operon has been found in a wide range of bacteria. We have previously identified the ter operon (terXYW and terZABCDEF) of the uropathogenic strain Escherichia coli KL53. In this study, we use an innovative approach to identify putative protein-protein interaction partners for one of the essential tellurite resistance proteins - TerB. We observe that N-terminus of TerB attaches to the periplasmic membrane, while the C-terminus is partly localized in the cytoplasm. Subsequently, by methods of in vivo cross-linking and mass-spectroscopic analysis, we have determined the proteins from both the membrane and cytoplasmic fractions, which can potentially interact with TerB.
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