Fig. 2: NMR analysis of the mixing of Lin28 and YB-1 on single-stranded nucleic acids. | Communications Biology

Fig. 2: NMR analysis of the mixing of Lin28 and YB-1 on single-stranded nucleic acids.

From: Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain

Fig. 2

a Two-dimensional 1H-15N HSQC spectra of Lin28-CSD (32–136 aa.) in free state or in presence of 10 nt-long poly(C) oligonucleotides. b Lin28-CSD and YB-1-CSD residues perturbed upon binding to 10-nt-long ssDNA (in gold and red, respectively). The residues are colored differently depending on their location: gray - β-sheet 1, blue - β-sheet 2, orange - β-sheet 3, yellow - loop 4, violet – loop 3 and CTD. c Gel mobility shift assays of a 20-nt long Poly(C) DNA in the presence of YB-1-CSD and Lin28-CSD. The protein/DNA molar ratios are indicated. Proteins were premixed in a buffer solution containing Tris 20 mM, pH 7.6, NaCl 40 mM, DTT 0.5 mM, then DNA was added at room temperature for 30 min. d Left panel: Two-dimensional 1H-15N HSQC spectra of Lin28-CSD in the presence of 20 nt-long ssDNA and TDP-43 RRM2 or YB-1-CSD in excess. Right panel: Height ratio of Lin28-CSD resonances in presence of 20 nt-long poly(C) DNA with/without TDP-43 RRM-2 or YB-1-CSD.

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