|
Figure 5.
FIGURE 5. Conservation correlates with the strength of
synthetic defects with pob3-Q308K. Top, residues that are
identical among at least 70% of the 31 Spt16 homologs aligned
(see Fig. 1) are indicated in red, revealing clustering near the
canonical binding/active site cleft for prolidase, methionine
aminopeptidase, aminopeptidase P, and creatinase (asterisk). The
full surface is shown on the left, and the loop residues 266-274
are removed in the middle panel to reveal the enclosed tunnel
region. The right panel shows a view rotated 180° about the
vertical axis. Bottom, severity of the synthetic defect when
combined with pob3-Q308K is indicated (Table 2); severe defects
are shown in red, moderate defects in orange, and mild defects
in yellow. If residues were tested individually and in multiple
mutations, only the score from the single mutation is used here.
Otherwise, the score for the complex mutation is assigned to all
residues altered. WT sequences are indicated along with the
number of the first residue. The orientations are the same as in
the top panels.
|
