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. 2009 Apr 16;28(10):1466–1478. doi: 10.1038/emboj.2009.92

Figure 6.

Figure 6

A positive-charged region of Sua5p is crucial for its function. (A) Modelled 3D structure of S. cerevisiae Sua5p. The modelled structure of S. cerevisiae Sua5p (green) is aligned with the template structure of S. tokodaii Sua5p (grey). (B) The relative protein surface potential is predicted and displayed with PyMOL software. A positive-charged region at the interface of yrdC and SUA5 domains is shown. (C) The point mutation in the positive-charged surface region of Sua5p affects its telomere maintenance function. Representative mutants, including K93A, R95A, D98K, R248A and R414D in the positive-charged region and S107F outside the positive-charged region, are pointed out in the upper panel. The mutant telomere lengths were examined (lower panel). (D) The point mutation in the positive-charged region of Sua5p abolishes its DNA-binding ability. 1 μM of wild-type or mutant Sua5 protein was used, and 50-fold excess of the random-sequence oligos were added into each reaction as competitor (upper panel). The purified wild-type and mutant Sua5 proteins are shown by Coomassie blue stained gel (lower panel).