• Boris Fürtig

New Publication: NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4

Together with members from the Schwalbe Lab we solved the solution state structure of the RNA binding domain of ribosomal protein S1.

We solved the NMR solution structure of the minimal mRNA-binding fragment of Vibrio Vulnificus rS1 containing the domains D3 and D4. Both domains are homologues and adapt an oligonucleotide-binding fold (OB fold) motif. NMR titration experiments reveal that recognition of miscellaneous mRNAs occurs via a continuous interaction surface to one side of these structurally linked domains. Using a novel paramagnetic relaxation enhancement (PRE) approach and exploring different spin-labeling positions within RNA, we were able to track the location and determine the orientation of the RNA in the rS1–D34 bound form.

The novel NMR tools to map transient interaction surfaces developed in this contribution will be of importance for other RNA–protein complexes.

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