Abstract
Lon is an ATPases associated with diverse cellular activities protease and belongs to a unique group that binds DNA. The α sub-domain of Lon protease is responsible for DNA-binding, but the structural information for its DNA-recognition mode is still limited. Here, we report 1H, 15N and 13C backbone assignment for the α sub-domain from Brevibacillus thermoruber Lon protease as the basis for the elucidation of its structure and interactions with DNA, necessary for understanding the allosteric regulatory mechanism of the enzymatic function.
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Acknowledgments
The NMR spectra were obtained at NMR facility of instrumentation center in NTU and High-Field Nuclear Magnetic Resonance Center (HF-NMRC) supported by the National Research Program for Genomic Medicine. This work was supported by the National Science Council (NSC99-2119-M-002-010) and National Taiwan University (NTU-ERP-101R8600-1 and NTU-ICRP-102R7560-5) to C.-H. Hsu.
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Chen, YD., Wu, SH. & Hsu, CH. Backbone resonance assignments of the α sub-domain of Brevibacillus thermoruber Lon protease. Biomol NMR Assign 8, 233–236 (2014). https://doi.org/10.1007/s12104-013-9490-6
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DOI: https://doi.org/10.1007/s12104-013-9490-6