TABLE 1.
Repression | Biotin requirementa | Mutation siteb | Secondary structurec | OmpR mutantd | Reference |
---|---|---|---|---|---|
nm | |||||
+ | 1.6 | None | Ref. 16 | ||
++ | 1.6 | T52S | Wing | This study | |
+ | 1.6 | T52I | Wing | T224I | This study |
+ | 1.6 | V53A | Wing | This study | |
+ | 1.6 | V53M | Wing | This study | |
+ | 1.6 | G55S | Wing | This study | |
− | 1.6 | G57S | Wing | G229S | This study |
− | 1.6 | Y58F | Wing | This study | |
+ | 1.6 | Y58T | Wing | This study | |
− | 41–4000 | Δ2–65 | wHTH | Ref. 11 | |
− | 41–4000 | Δ2–63 | wHTH | Ref. 12 | |
− | 41–4000 | Δ3–60 | wHTH | This study | |
− | 41–4000 | Δ3–40 | Helix I, II, III | This study | |
− | 41–4000 | Δ3–25 | Helix I, II | This study | |
− | 41–4000 | Δ48–61 | ΔWing | This study | |
− | 1.6 | 50–62 substitution | Chimera | This study | |
− | 4000 | G115S | BBLe | Refs. 15 and 19 | |
− | 41–4000 | R118G | BBL | Ref. 16 | |
− | 4 | R119W | BBL | Ref. 16 |
a The minimal biotin requirements of the deletion and the point mutants constructed in this study. The data for the N-terminal mutants are directly from Refs. 15, 16, and 19.
b Positions are amino acid residue positions.
c Locations of the mutations in the secondary structure of BirA protein.
d Wing residue substitutions having regulatory effects in the OmpR system.
e BBL, biotin binding loop.