1. Alignment of Stau dsRBDs.
Alignment of Stau dsRBDs. (A) Multiple sequence alignment of all dsRBDs present in Stau proteins from D. melanogaster (d) or Homo sapiens (h). The number of residues present in the insertion within dsRBD2 is indicated in square brackets, the sequence is omitted. Each Stau dsRBD is more similar to the corresponding dsRBD in another Stau homolog than to another dsRBD within the same protein. (B) Sequence comparison of Stau dsRBDs 3 and 4 (from Drosophila and humans) with various known RNA-binding dsRBDs from other human (h), Aquifex aeolicus (a), or X. laevis (Xl) proteins. Red circles: hStau1 residues involved in contact with the backbone of ARF1 SBS; red triangles: hStau1 residues involved in base-directed contacts with ARF1 SBS; blue diamonds: hStau1 residues mediating the interaction between dsRBD3A and dsRBD4 observed in our complex; black triangles: position of residues involved in base-specific contacts with the RNA for other dsRBDs present in the alignment (see also Fig S8). Alignments were generated with T-Coffee Expresso (Armougom et al, 2006) and manually optimized considering structural information available in the PDB database or, in its absence, PsiPred secondary structure predictions (McGuffin et al, 2000). The secondary structure of hStau1 dsRBDs 3 (dark blue) and 4 (cyan) is schematized above the alignment; arrows: β-sheets; helices: α-helices; dotted lines: residues not visible in the electron density. Numbers on top indicate residue positions in the alignment (related to Fig 1).
Daniela Lazzaretti et al. LSA 2018;1:e
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