NMR assignments of the N-terminal signaling domain of the TonB-dependent outer membrane transducer PupB
Outer membrane TonB-dependent transducers (TBDTs) actively transport ferric siderophore complexes from the extracellular environment into Gram-negative bacteria. They also participate in a cell-surface signaling regulatory pathway that results in upregulation of the transducer itself, in response to iron-deplete conditions. The TBDT PupB transports ferric pseudobactin, and signals through its N-terminal signaling domain (NTSD), while the TBDT homolog PupA is signaling-inactive. Here, we report the NMR chemical shift assignments of the PupB-NTSD. This information will provide the basis for structural characterization of the PupB-NTSD to further explore its signaling properties.
KeywordsCell surface signaling Ton-B dependent transporters Pseudomonas Pseudobactin Nuclear magnetic resonance
The authors thank Dr. John Bagu, NDSU Organic Spectroscopy lab, for assistance with in-house HSQC experiments and Dr. Sangita Sinha for critical reading of the manuscript. This research was supported in part by the National Institutes of Health (NIH) National Institutes of General Medical Science (NIGMS) (1R15 GM113227) to CLC, the NIH National Center for Research Resources (2P20 RR015566), and the NIH NIGMS (P30 GM103332). JLJ was supported by the North Dakota Experimental Program to Stimulate Competitive Research Doctoral Dissertation Assistantship (#FAR0025216). The Biomolecular NMR facility at UTSW acknowledges National Institutes of Health grants S10 RR026461-01 for its 600 MHz Agilent DD2 console and National Institutes of Health Grant 1S10OD018027-01 for its 800 MHz Agilent D22 console.
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