TABLE 2.
In vivo functionality of altered P22 scaffolding proteins
| Mutanta | Average induction titerb | Bacterial strainc |
|---|---|---|
| Wild-type | 3 × 1010 | UB-1757 |
| Wild-type | 9 × 1010 | UB-1790 |
| N272D | 1 × 1011 | UB-1971 |
| I276D* | 1 × 107 | UB-1968 |
| M280D* | 5 × 1010 | UB-1780 |
| A283D* | 6 × 103 | UB-1787 |
| A284D† | 6 × 103 | UB-1779 |
| S285D† | 2 × 1010 | UB-1810 |
| G287D† | <105 | UB-1813 |
| G287P† | × 108 | UB-1811 |
| G287A† | 1 × 1010 | UB-1799 |
| V289D | <105 | UB-1808 |
| V289A | 7 × 109 | UB-1784 |
| T291D | 4 × 1010 | UB-1783 |
| Y292D* | 1 × 104 | UB-1788 |
| L295D* | <104 | UB-1901 |
| L299D* | <104 | UB-1972 |
| I302D | 1 × 1011 | UB-1970 |
| N272D, I267R, | <104 | UB-2018 |
| L299D |
a Scaffolding protein changes are shown. Asterisks (*) mark the amino acids whose side chains are participants in the HTH zipper of hydrophobic core of the scaffolding protein, and daggers (†) mark those in the β1-turn.
b Average of two or more determinations as described under “Experimental Procedures.”
c Mutations were constructed in a P22 15−ΔSC302::KanR, 13−amH101 prophage (except UB-1968, UB-1970–2, UB-1790, UB-1901, and UB-3018, which were in P22 ΔsieA-1, 15−ΔSC302::KanR, 13−amH101) as described under “Experimental Procedures.”