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. 2012 Aug 9;287(40):33766–33780. doi: 10.1074/jbc.M112.393132

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 15ΔSC302::KanR, 13amH101 prophage (except UB-1968, UB-1970–2, UB-1790, UB-1901, and UB-3018, which were in P22 ΔsieA-1, 15ΔSC302::KanR, 13amH101) as described under “Experimental Procedures.”