The multiple Tudor domain-containing protein TDRD1 is a molecular scaffold for mouse Piwi proteins and piRNA biogenesis factors

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FIGURE 5.
FIGURE 5.

Overall architecture of the TD1–4 domains of TDRD1 as determined from small-angle scattering data. (A) TD1–4 ab initio models showing “most representative (filtered)” (gray) and “average” envelope (light blue) as given by DAMAVER. The rigid body model was produced using CORAL (Petoukhov and Svergun 2005). TD1 (salmon), TD2 (light red), and TD4 (deep blue) models were based on Tudor-SN (pdb code 2WAC). TD3 (light blue) was fitted using the crystal structure determined here. Flexible linkers connecting the eTud domains, positioned by CORAL, are depicted as spheres (olive green). (B) Ab initio model (orange) derived from the TD1-2 SAXS data. This is consistent with either half of the TD1–4 model. (C) SAXS data (black dots with error bars) and fits for TD1–4 and TD1–2 (solid lines). (Top) TD1–4 data. Fit of the ab initio model shown in A (gray) and the multidomain model created by CORAL (purple). (Bottom) TD1–2 data. Fit of the ab initio model shown in B (orange). Fits of the tandem TD1–2 and TD3–4 parts of the CORAL model are, respectively, shown in red and blue.

This Article

  1. RNA 18: 2056-2072