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. 2009 Apr 8;106(17):6939–6944. doi: 10.1073/pnas.0900833106

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Fig. 5. — Both elongation and hydrophilicity of the side chain at residue 198 are required to convert Aurora-A into Aurora-B-like kinase. (A) Aurora-A and -B are distinguished by different partner proteins through local structural change at a single amino acid. (i and ii) The complex of human Aurora-A^122–403/TPX2^1–43 (PDB ID code 1OL5 in ref. 14). (v and vi) The complex of Xenopus Aurora-B^78–361/INCENP^798–840 (PDB ID code 2BFY in ref. 37). (iii, iv, vii, and viii) Predicted by point mutation using PyMol (www.pymol.org). Structurally, G198 of Aurora-A (green) interacts with TPX2^P13 (blue) in 3-dimensional space (i and ii). When G198 is replaced by N, the side chain is elongated, and TPX2 is prevented from Aurora-A (iii and iv). In contrast, Aurora-B (yellow) interacts with INCENP (purple) in a looser way within the equivalent domain (v and vi). The side chain of N158 in Xenopus Aurora-B interacts perfectly with INCENP^{Y825/I828/D829/S830} and forms hydrogen bonds with INCENP^Y825/I828. Thus, Aurora-A^G198N can interact with INCENP through its N198, which not only fits the 3-dimensional structure but probably builds hydrogen bonds with human INCENP^I872 (vii and viii). (B) Overview of Aurora-A localization after substituting G198 with various amino acids. When the length of side chain reached that of V and L, Aurora-A was prevented from spindle. Hydrophilic side chains N and Q localized Aurora-A to centromere and midzone. (C) HeLa cells were transfected with GFP-tagged Aurora-A^WT, Aurora-A^G198A, Aurora-A^G198V, Aurora-A^G198L, Aurora-A^G198N, or Aurora-A^G198Q (Left, and green in Right), and subjected to immunofluorescence microscopy. DNA labeled with DAPI (Center, and blue in Right). Arrows indicate centromere and midzone. (Scale bar, 10 μm.) (D) GFP-tagged Aurora-A^G198A, Aurora-A^G198V, Aurora-A^G198L, Aurora-A^G198N, or Aurora-A^G198Q was transfected into HeLa cells and immunoprecipitated from cell lysate with GFP antibody. The immunoprecipitated complexes were blotted for INCENP (Upper) or GFP (Lower). Aurora-A^G198N and Aurora-A^G198Q bound INCENP, whereas Aurora-A^G198A, Aurora-A^G198V, and Aurora-A^G198L did not.