Table 5.

Ability of t-BOOH to promote dissociation of σ^E-ChrR complexes containing wild type or variant ChrR proteins in vivo¹.

ChrR Protein	Before t-BOOH	After t-BOOH	Fold Change
WT	19 ± 3	173 ± 64	9.1
ChrR85	34 ± 6	45 ± 7	1.3
H141A	25 ± 2	44 ± 9	1.7
H143A	31 ± 4	38 ± 2	1.2
E147A	20 ± 4	25 ± 6	1.3
H177A	40 ± 8	50 ± 9	1.3
C187A	44 ± 6	82 ± 14	1.9
C189A	27 ± 8	64 ± 12	2.4
C187S	109 ± 26	256 ± 75	2.3
C189S	60 ± 9	262 ± 83	4.4

¹Shown are the differential rates of β-galactosidase synthesis measured from an rpoE∷lacZ operon fusion that requires σ^E in cells containing the indicated ChrR protein as their sole source of this anti-σ factor before or after addition of 100 µM t-BOOH. The column labeled fold change reports the ratio of these rates before and after addition of 100 µM t-BOOH.