Abstract
The protein SP_0782 from Streptococcus pneumonia is a small homodimeric protein that belongs to a protein family containing representative members with single-stranded DNA (ssDNA) binding functions. The ssDNA binding of the homolog YdbC from Lactococcus lactis was previously characterized when bound to a 20-mer of pyridine-rich ssDNA, sharing an overall similar structural fold with the human transcription coactivator PC4. We report that SP_0782 exhibits distinct differences in ssDNA binding properties from YdbC as revealed by NMR titration experiments. Unlike the binding of the ssDNA dT19G1 to PC4 and YdbC, SP_0782 resulted in aggregation. In addition, SP_0782 exhibits favorable binding to shorter ssDNA such as dT6. The reason is unclear, and the SP_0782 structure–function relationship remains to be elucidated. Here, we report the complete 1H, 13C, and 15N backbone and side chain NMR assignments of SP_0782, residues 7–79.
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Acknowledgments
This work was supported by Protein Structure Initiative-Biology Program by the National Institute of General Medical Sciences (Grant Numbers: U54-GM074958 and U54-GM094597), the Hundred Talent Program by Chinese Academy of Sciences, the Ministry of Science and Technology (Grant number 2016YFA051201), and the National Natural Sciences Foundation of China (Grant Number: 21575155). We thank all personnel at the Rutgers protein production facility for sample preparation and technical support. All NMR data collection was conducted at the Ohio Biomedicine Center of Excellence in Strucstural Biology and Metabonomics at Miami University.
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Li, S., Ramelot, T.A., Kennedy, M.A. et al. Chemical shift assignments of the homodimer protein SP_0782 (7–79) from Streptococcus pneumoniae . Biomol NMR Assign 10, 341–344 (2016). https://doi.org/10.1007/s12104-016-9697-4
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DOI: https://doi.org/10.1007/s12104-016-9697-4