Fig. 4: Peptide from UPF1 binds to LIN28A.

a Schematic of deletional GST-MYC-UPF1 variants. CH, Helicase, and SQ represent the cysteine-histidine-rich domain, helicase activity domain, and serine-glutamine-rich domain, respectively. Various proteins interacting with UPF1 domains are indicated. Dots indicate phosphorylation sites on UPF1. b Each UPF1 variant in (a) and pFLAG-LIN28A was co-transfected in 293T cells followed by GST pull-down in the presence of nuclease mixture. WB was performed to evaluate the expression of deletional variants and eluates. c Eight polypeptides, including one random sequence peptide (P1) and seven peptides (P2–P8) from UPF1 (419–700), were depicted with amino acid sequences. Seven peptides (P2–P8) are represented on the UPF1 structure (PDB: 2wjy, 419–700 was displayed with cartoon style). d Kinetics evaluations of P8 using SPR analysis were performed at various concentrations. The minimum number of independent biological replicate experiments was b n = 3. The experiments were conducted three times, each iteration producing consistent results.