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. 2006 May 18;25(11):2564–2574. doi: 10.1038/sj.emboj.7601141

Figure 5.

Figure 5

Sws1 is a conserved protein and the SWIM domain is required for its function. (A) Four-fold serial dilutions of wt (PR109), sws1Δ (VM3723), sws1-C152S (VM3734), rqh1Δ (SC3250), sws1Δ rqh1Δ (VM3722) and sws1-C152S rqh1Δ (VM3733) were plated on YES plates (control), YES plates supplemented with 3 mM HU or 0.02% MMS, or YES plates that afterwards were treated with 300 Gy of IR. Photographs were taken after 4 days at 32°C. (B) Model of the Zn-binding region of the SWIM domain in Sws1. The three cysteine residues and the histidine residue predicted to be involved in Zn chelation are indicated. The cysteine residue (Cys152) mutated in sws1-C152S is underlined. (C) Alignment of Sws1 and its orthologs from H. sapiens, M. musculus, A. thaliana, C. albicans and S. cerevisiae. The conserved CxC(x)nCxH motif and secondary structure elements (upstream β-strands and the downstream α-helix) are shown.