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. 2024 Jul 14;300(8):107571. doi: 10.1016/j.jbc.2024.107571

Figure 2.

Figure 2

Conservation and location of the Leu187 residue in the EXOSC4/Rrp41 subunit of the RNA exosome that is altered in disease.A, a cartoon model of the 10-subunit RNA exosome complex is shown. The subunits of the complex are indicated by their EXOSC number (1–3 in the cap, 4–9 in the barrel-like core ring), with the catalytic DIS3 subunit at the base. EXOSC4 (Rrp41 in budding yeast), which is a component of the barrel-shaped core ring structure, is highlighted in teal and the proximal subunit EXOSC9 (Rrp45 in budding yeast) is highlighted in slate blue. B, schematic of domain organization of EXOSC4. EXOSC4 is composed of a single RNase PH-like domain. Alignment of EXOSC4/Rrp41 amino acid sequences from Homo sapiens (H.s.), Mus musculus (M.m.), Drosophila melanogaster (D.m.), and Saccharomyces cerevisiae (S.c.) below the schematic show the conservation of the Leu187 residue (magenta). C, structural model of the human RNA exosome complex (PDB: 6D6R) (27) and (D) budding yeast RNA exosome complex (PDB: 6FSZ) (30). The zoomed in boxes in (C and D) depict the RNA exosome subunits EXOSC4/Rrp41 (teal) and EXOSC9/Rrp45 (slate blue) that share an interface and show the location of the Leu187 residue (magenta) in EXOSC4/Rrp41. The EXOSC4/Rrp41 residue Leu199 (teal) and the EXOSC9 residue Ile234/Rrp45 residue Val248 (slate blue) in close contact with the EXOSC4/Rrp41 residue Leu187 are shown.