Study of membrane attachment and in vivo co-localization of TerB protein from uropathogenic Escherichia coli KL53

作者：Alekhina Olga; Valkovicova Lenka; Turna Jan^*

来源：General Physiology and Biophysics, 2011, 30(3): 286-292.

DOI：10.4149/gpb_2011_03_286

• Tellurite resistance
• Amphitropic protein
• Cross-linking
• TerB protein

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.

• 出版日期2011-9