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. 2021 Sep 24;15(9):e0009810. doi: 10.1371/journal.pntd.0009810

Fig 1. DEAD box RNA helicase interacts with HspN and may facilitate base pairing interaction with HspC complementary sequence.

Fig 1

A) Schematic representation of RNA-protein pulldown experiment. B) Silver stained 8% SDS-PAGE showing specific nuclear proteins pulled—down with biotinylated pre-mRNAs- HspN, HspNΔ26, HspC, HspCΔ27 (Lanes 1–4). Biotinylated FL Hsp90 and bead alone (BA) in lanes 5 and 6 serve as negative controls. 10% input (lane 7) shows proteins in the nuclear extract. Unique bands obtained after the RNA-Protein pull down assay, marked in the Figure, were cut, and processed further for mass spectrometric identification of RNA binding proteins. ATP dependent RNA helicase DHR1 was identified from the middle intense band highlighted explicitly using a box, among the three intense bands pulled down with wild type HspN in Lane 1. Other unique proteins pulled down with HspN (lane 1) in the other two bands, proteins pulled down with HspNΔ26, HspC and HspCΔ27 are subject matter for future research. C) Schematic representation describing the different domains of Giardia RNA helicase identified to be interacting with HspN pre-mRNA. The protein-protein blast with pre-mRNA splicing factor, ATP dependent RNA helicase- PRP16 of S. pombe revealed the presence of DEAD/H box helicase motif between 348–351 aa which was previously not annotated.