Backbone resonance assignments of the C-terminal region of human translation initiation factor eIF4B

International audienceTranslation 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

Construction of a <em>Mycoplasma feriruminatoris</em> chassis for the development of a vaccine for contagious caprine pleuropneumonia

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Construction of a <em>Mycoplasma feriruminatoris</em> chassis for the development of a vaccine for contagious caprine pleuropneumonia

International audienc

Extension of synthetic biology methods for the genome engineering of<em> Mycoplasma feriruminatoris</em>

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Development of a novel vaccine for contagious caprine pleuropneumonia based on a fast-growing <em>Mycoplasma feriruminatoris</em> chassis

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