Abstract
Translation initiation in eukaryotes is an early step in protein synthesis, requiring multiple factors to recruit the ribosomal small subunit to the mRNA 5’ untranslated region. One such protein factor is the eukaryotic translation initiation factor 4B (eIF4B), which increases the activity of the eIF4A RNA helicase, and is linked to cell survival and proliferation. We report here the protein backbone chemical shift assignments corresponding to the C-terminal 279 residues of human eIF4B. Analysis of the chemical shift values identifies one main helical region in the area previously linked to RNA binding, and confirms that the overall C-terminal region is intrinsically disordered.
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The assignments have been deposited to the BMRB under accession codes 51952, 51953 and 51957.
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Acknowledgements
The authors would like to thank Estelle Morvan, Axelle Grélard, and the IECB biophysical and structural chemistry facility (CNRS UAR3033, Inserm US001, Univ. Bordeaux), for NMR support and access to the 700 MHz spectrometer. We thank Jean-Michel Blanc and the IECB biochemistry facility for assisting the preparation of the initial eIF4B CTR plasmid.
Funding
This work was supported by grants from the Fondation pour la Recherche Médicale (AJE20171239128 to MA), Junior Chair IdEx Univ. Bordeaux (OPE-2018-0405 to MA), ANR JCJC (DISTINCT: ANR-20-CE11-0007 to MA), and recurrent funds from the French National Institute of Medical Research (Inserm; MA, CDM).
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SR created the plasmids. SR, VT and CABT expressed and purified the protein samples. CDM collected and processed the NMR data. SM, CABT and CDM analyzed the NMR data. MA and CDM directed the project and wrote the manuscript.
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Mondal, S., Rousseau, S., Talenton, V. et al. Backbone resonance assignments of the C-terminal region of human translation initiation factor eIF4B. Biomol NMR Assign 17, 199–203 (2023). https://doi.org/10.1007/s12104-023-10141-7
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DOI: https://doi.org/10.1007/s12104-023-10141-7