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. 2021 Jan 18;12:428. doi: 10.1038/s41467-020-20481-w

Fig. 1. SRSF1 RRM1 interaction with the AACAAA RNA.

Fig. 1

A The sequence of recombinant SRSF1 protein used in this study is shown. Amino acid numbering is according to the PDB sequence. Amino acids involved in the formation of β-strands and α-helices are colored in red and green, respectively. B Superimposition of 1H-15N HSQC spectra obtained with 15N-labeled SRSF1 RRM1 and increasing amount of unlabeled 5’-AACAAA-3’ RNA. The titration was performed at 40 °C (313 K), in the NMR buffer. The peaks corresponding to the free and RNA-bound states (RNA:protein ratios of 0.3:1 and 1:1) are colored blue, orange, and red, respectively. The highest chemical-shift perturbations observed upon RNA binding are indicated by black arrows. C Representation of the combined chemical-shift perturbations (∆δ = [(δ HN)2 + (δN/6.51)2]1/2) of SRSF1 RRM1 amides upon binding to 5’-AACAAA-3’ RNA, as a function of RRM1 amino acid sequence. Secondary-structure elements of the protein domain are displayed at the bottom of the graph.