Extended Data Fig. 5: Changes in thermal stability of essential proteins. | Nature

Extended Data Fig. 5: Changes in thermal stability of essential proteins.

From: The functional proteome landscape of Escherichia coli

Extended Data Fig. 5

a, log2-transformed fold change of FtsK protein levels in each mutant compared to control at each temperature. FtsK is strongly thermally destabilized in the ΔphoP mutant and the ftsK knockdown is synthetically lethal with the phoP deletion (Fig. 2d). b, As in a for parC. ParC is strongly thermally stabilized in the ΔclpS mutant and thermally destabilized in the ΔphoP mutant and the parC knockdown is synthetically lethal with both. Synthetic lethality is also apparent in the ΔahpC, ΔamiA and ΔenvC mutants, despite the absence in changes in ParC thermal stability (Fig. 2e).

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