Abstract
Homeodomain-containing transcription factors including Hox proteins play fundamental roles in the regulation of different cellular and developmental processes. These proteins all contain a homeodomain, which is a 60-amino acid DNA binding domain encoded by a 180-base pair DNA sequence. Homeodomains also serve as protein interaction targets to regulate the functions of these transcription factors or other proteins. The cell cycle regulator Geminin interacts with Hox homeodomains to inhibit the transcription activities of Hox proteins and enrolls Hox proteins in the cell proliferation process. Here we report complete chemical shift assignments of the homeodomain of Hoxc9 (Hoxc9-HD) in complex with the homeodomain binding region of Geminin (Gem-HBR), which were determined by triple resonance NMR experiments. These resonance assignments provide a basis for the structure determination of the Hoxc9-HD/Gem-HBR complex and for the further study of homeodomains in complex with other regulatory protein partners (BMRB deposits with accession number 17407).
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Acknowledgments
We thank Mr. R. Feng for setting up the NMR experiments; C. Liang for the Geminin cDNA. This work was supported by grants from Hong Kong Research Grants Council (RGC663911) and AoE/M-06/08.
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Zhou, B., Liu, C. & Zhu, G. 1H, 15N and 13C chemical shift assignments of the homeodomain of Hoxc9 in complex with the cell cycle regulator Geminin. Biomol NMR Assign 9, 165–168 (2015). https://doi.org/10.1007/s12104-014-9566-y
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DOI: https://doi.org/10.1007/s12104-014-9566-y