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. Author manuscript; available in PMC: 2022 Nov 26.
Published in final edited form as: Science. 2021 Nov 25;374(6571):1113–1121. doi: 10.1126/science.abe2913

Fig. 2: TNDs are selectively recognized by TND-interacting motifs (TIMs) conserved in transcription regulators.

Fig. 2:

(A) Multiple sequence alignments illustrating conserved TND-recognizing TIMs. (B) Interaction network of proteins containing a TND module or TIM. Edges represent interaction data from the STRING database and are weighted by the confidence score calculated by STRING. TIM-containing proteins are highlighted in bold. (C) Comparison of 2D 15N/1H SOFAST-HMQC NMR spectra of ELOA TND alone (yellow) or with an increasing amount of MED13 TIM (gradient of blue). (D) Quantification of chemical shift perturbation (CSP) in backbone amide signals of the ELOA TND upon titration with MED13 TIM from panel (C). (E) Determination of the dissociation constant (KD) for the ELOA-TND:MED13-TIM complex formation by NMR. Error bars represent the error of the fit for the most perturbed residues (n = 10). (F) Heatmap of the mean CSP of the 10% most affected residues for each TND:TIM binary interaction. (G) Interaction network reconstructed from TND:TIM binary interactions as determined by NMR. Line darkness indicates the strength of each pairwise interaction based on mean CSP values presented in panel (F). (H) Quantification of CSP for each TND:TIM combination at a 1:4 ratio. (I) Examples of CSP values from panel (H) highlighted on the surfaces of different TNDs.