Fig. 3: F125 and F128 are predicted to direct the prometaphase destruction of a pool of non-separase-bound excess securin. | Nature Communications

Fig. 3: F125 and F128 are predicted to direct the prometaphase destruction of a pool of non-separase-bound excess securin.

From: A prometaphase mechanism of securin destruction is essential for meiotic progression in mouse oocytes

Fig. 3

a Multiple sequence alignment of the region surrounding residues F125 and F128 (marked with asterisks) in securin orthologs. b The molecular surface of separase (green) in contact with the region of securin detailed in Fig. 3a (purple). Image generated using the crystal structure of the Saccharomyces cerevisiae separase-securin complex (PDB accession 5U1T [10.2210/pdb5U1T/pdb])18. The side chains of securin residues Y276 and F279, which correspond to F125 and F128 in the human protein, are shown as stick models and labelled in purple. The N- and C-termini of the securin segment displayed are also labelled in purple c Schematic representation of a tethered separase-securin complex reporter (separase-securin FL) including a cartoon demonstrating predicted complex interaction. d Mean VFP-tagged securin FL (magenta trace, n = 8) and separase-securin FL (green trace, n = 6) destruction profiles relative to PB1 extrusion.

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