title: Study of membrane attachment and in vivo co-localization of TerB protein from uropathogenic Escherichia coli KL53.
abstract: 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.
authors.affiliation: Department of Molecular Biology, Comenius University, Bratislava, Slovakia.
authors.forename: Olga
authors.initials: O
authors.lastname: Alekhina
authors.forename: Lenka
authors.initials: L
authors.lastname: Valkovicova
authors.forename: Jan
authors.initials: J
authors.lastname: Turna
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000737:chemistry / Q000494:pharmacology; D003593:Cytoplasm / Q000378:metabolism; D024881:Drug Resistance, Bacterial; D029968:Escherichia coli Proteins / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013347:Subcellular Fractions; D013691:Tellurium / Q000737:chemistry; D056689:Uropathogenic Escherichia coli / Q000235:genetics* / Q000378:metabolism
chemical_list: D003432:Cross-Linking Reagents; D029968:Escherichia coli Proteins; C119920:tellurite resistance protein B, E coli; C026660:tellurous acid; D013691:Tellurium