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. 2001 Apr;12(4):1161–1175. doi: 10.1091/mbc.12.4.1161

Figure 1.

Figure 1

Mutations designed to cover all residues involved with binding various ligands, e.g., the binding with actin (a), poly-l-proline (p), and PIP2 (+), marked on top of the wild-type S. pombe profilin sequence. Some residues may participate in both actin and PIP2 binding. Each point mutant is represented by the mutated amino acid that aligns with the wild-type sequence. E42K (*) is the mutation of profilin in cdc3-124 ts strain. C89S (*) is a control mutant for structure stability. Mutants that failed to complement both null (32°C) and ts (36°C) strains are bold and underlined; mutants that complemented the ts at 36°C but not the null strain at 32°C are bold only. Four of these noncomplementing mutants complement null strain at 25°C (i).