Abstract
hHR23a (human homolog of Rad23 a) functions in nucleotide excision repair and proteasome-mediated protein degradation. It contains an N-terminal ubiquitin-like (UBL) domain, an xeroderma pigmentosum C (XPC)-binding domain, and a ubiquitin-associated (UBA) domain preceding and following the XPC-binding domain. Each of the four structural domains are connected by flexible linker regions. We report in this NMR study, the 1H, 15N and 13C resonance assignments for the backbone and sidechain atoms of the hHR23a full-length protein with BioMagResBank accession number 52059. Assignments are 97% and 87% for the backbone (NH, N, C′, Cα, and Hα) and sidechain atoms of the hHR23a structured regions. The secondary structural elements predicted from the NMR data fit well to the hHR23a NMR structure. The assignments described in this manuscript can be used to apply NMR for studies of hHR23a with its binding partners.
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Data availability
Assignments hHR23a have been deposited in the BMRB under accession code 52059. The plasmid for generation of hHR23a as used in this study is available upon request.
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Acknowledgements
NMR data were acquired at the NMR facility of the University of Minnesota.
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This research was funded by the Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research to K.J.W. (1 ZIA BC011490).
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XC and KJW designed and performed the experiments, analyzed the data, prepared all figures and wrote the manuscript. XC deposited the assignments in the BMRB.
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Chen, X., Walters, K.J. 1H, 15N, 13C resonance assignments for proteasome shuttle factor hHR23a. Biomol NMR Assign 17, 287–291 (2023). https://doi.org/10.1007/s12104-023-10157-z
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DOI: https://doi.org/10.1007/s12104-023-10157-z