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. 2015 Sep 24;6:776. doi: 10.3389/fpls.2015.00776

Figure 8.

Figure 8

Candidate proteins associated with colonization of the environment identified based on high sTEKhot values. (A) Multiple protein sequence alignment of B. cinerea BC1G_03854 (sTEKhot = 4.29), S. borealis SBOR_9046 (sTEKhot = 10.01), S. sclerotiorum SS1G_10836 (sTEKhot = 7.34) and the hyperactive Type I antifreeze protein “Maxi” from Pseudopleuronectes americanus (4KE2_A). (B) Superimposition of Maxi antifreeze protein structure (tan) and SS1G_10836 model structure (rainbow). (C) Surface hydrophobicity of SS1G_10836 model dimer. Dotted line corresponds to the position of the section shown on the right, illustrating the characteristic hydrophilic inner core of the dimer. (D) Multiple protein sequence alignment of B. cinerea BC1G_07573 (sTEKhot = 7.07), S. borealis SBOR_1255 (sTEKhot = 3.79), S. sclerotiorum SS1G_03146 (sTEKhot = 1.58) and the AA11 Lytic Polysaccharide Monooxygenase from Aspergillus oryzae (4MAH_A). (E) Superimposition of A. oryzae AA11 structure (tan) and SS1G_03146 model structure (rainbow). (F) SS1G_10836 and SS1G_03146 gene expression in vitro (PDB, Potato Dextrose Broth), during colonization of Arabidopsis thaliana (lesion periphery and lesion center) and in sclerotia. Error bars show standard error of the mean from two independent biological replicates.