Journal
ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY
Volume 104, Issue 6, Pages 899-911Publisher
SPRINGER
DOI: 10.1007/s10482-013-0009-z
Keywords
Tellurite resistance; Ter proteins; Pull-down assay; Protein-protein association; Protein localization; Escherichia coli
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Funding
- VEGA Grant from the Ministry of Education of the Slovak Republic [1/0346/10]
- Slovak Research and Development Agency [APVV-20-054005]
- Comenius University Grant [UK/560/2010]
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Gene cluster ter conferring high tellurite resistance has been identified in various pathogenic bacteria including Escherichia coli O157:H7. However, the precise mechanism as well as the molecular function of the respective gene products is unclear. Here we describe protein-protein association and localization analyses of four essential Ter proteins encoded by minimal resistance-conferring fragment (terBCDE) by means of recombinant expression. By using a two-plasmid complementation system we show that the overproduced single Ter proteins are not able to mediate tellurite resistance, but all Ter members play an irreplaceable role within the cluster. We identified several types of homotypic and heterotypic protein-protein associations among the Ter proteins by in vitro and in vivo pull-down assays and determined their cellular localization by cytosol/membrane fractionation. Our results strongly suggest that Ter proteins function involves their mutual association, which probably happens at the interface of the inner plasma membrane and the cytosol.
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