TABLE 3.
Effects of deletions in FliM on its function and binding to other proteinsa
| FliM construct | Protein segment(s) remaining | Phenotype | Binding to:
|
|||
|---|---|---|---|---|---|---|
| FliN | FliG | CheY | CheY-P | |||
| WT FliM |  |
WT | + | + | + | + |
| Δ1–38 | Che− | + | + | +/− | +/−− | |
| Δ1–60 | Fla− | + | + | +/− | +/−− | |
| Δ61–144 | Fla− | + | + | + | ++ | |
| Δ145–241 | Fla− | +/− | +/− | + | ++ | |
| Δ241–334 | Fla− | − | +/− | +/− | ++ | |
| Δ1–241 | Fla− | + | ND | ND | ND | |
| Δ145–334 | ND | ND | + | +/− | +/− | |
| Δ1–247 | ND | + | + | + | +/− | |
a Summary of FliM deletions studied, their phenotypes, and the binding of FliM fragments to FliN, FliG, CheY, and phospho-CheY. Phenotypes of the deletions were determined by expressing the proteins in the fliM null strain DFB190. Binding was examined in coprecipitation experiments using the one-cell protocol and induction by 200 μM IPTG (interactions with FliN or FliG) or the two-cell protocol and induction by 100 μM IPTG (interactions with CheY or phospho-CheY). The symbols ++, +, +/−, and +/−− indicate four levels of binding, differing from each other by a factor of about 2 in the amount of coprecipitated FliM; ND, not determined; WT, wild type. Broken lines indicate internal deletions in FliM.