Abstract
CISD3 is a mitochondrial protein that contains two [2Fe–2S] clusters. This protein is overexpressed in some types of cancer, so it has emerged as a potential drug target. A detailed characterization of this protein is crucial to understand how CISD3 is involved in these physiopathologies. In this study, isotopically labeled human CISD3 was expressed in Escherichia coli. A set of double and triple resonance experiments performed with standard parameters/datasets provided the assignment of 40% of the HN resonances, 47% of Cα, and 46% of C′ resonances. Tailored paramagnetic HSQC, CON and CACO experiments extended up to 59% for HN, 70% for Cα and 69% for C′. The 1H, 13C and 15N NMR chemical shift assignment of human CISD3 is reported here.
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Assignment deposited in BMRB, ID 51439. Raw data deposited in BMRBig, ID bmrbig82.
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Acknowledgements
The authors acknowledge the support by the Italian Ministry for University and Research (FOE funding) to the CERM/CIRMMP Italian Centre of Instruct-ERIC, a landmark ESFRI project. JMS acknowledges a Fellowship from TIMB3, Grant No. 810856, funded by the Horizon 2020 research and innovation program of the European Commission. DG is a PhD student supported under the EOSC-Life Project (ID:824087) funded by the Horizon 2020 EC program.
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JMS and MP wrote the manuscript, JMS and FC prepared figures; JMS, DG and FC performed the assignment; all authors reviewed the manuscript.
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Silva, J.M., Grifagni, D., Cantini, F. et al. 1H, 13C and 15N assignment of the human mitochondrial paramagnetic iron–sulfur protein CISD3. Biomol NMR Assign 17, 17–22 (2023). https://doi.org/10.1007/s12104-022-10113-3
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DOI: https://doi.org/10.1007/s12104-022-10113-3