Abstract
Vibrio cholerae is the bacterial causative agent of the human disease cholera. Non-pathogenic bacterium can be converted to pathogenic following infection by a filamentous phage, CTXΦ, that carries the cholera toxin encoding genes. A crucial step during phage infection requires a direct interaction between the CTXΦ minor coat protein (pIIICTX) and the C-terminal domain of V. cholerae TolA protein (TolAIIIvc). In order to get a better understanding of TolA function during the infection process, we have initiated a study of the V. cholerae TolAIII domain by 2D and 3D heteronuclear NMR. With the exception of the His-tag (H123–H128), 97 % of backbone 1H, 15N and 13C resonances were assigned and the side chain assignments for 92 % of the protein were obtained (BMRB deposit with accession number 25689).
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Acknowledgments
Financial support from the TGIR-RMN-THC FR3050 CNRS for conducting the research is gratefully acknowledged. The authors thank the proteomic platform of the Institut de Microbiologie de la Mediterranée for mass spectrometry analysis and N-terminal sequencing.
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Navarro, R., Bornet, O., Houot, L. et al. 1H, 15N and 13C resonance assignments of the C-terminal domain of Vibrio cholerae TolA protein. Biomol NMR Assign 10, 311–313 (2016). https://doi.org/10.1007/s12104-016-9690-y
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DOI: https://doi.org/10.1007/s12104-016-9690-y