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The Escherichia coli RelB antitoxin C-terminus is essential for RelE toxin suppression and transcriptional repression.

ABSTRACT: Bacterial type II toxin-antitoxin (TA) systems exhibit high specificity within each pair to ensure precise recognition of the toxin by its cognate antitoxin to inhibit toxicity of the free toxin. Despite high structural similarity among some TAs, crosstalk between noncognate TA pairs is rare. To determine how the E. coli RelB antitoxin suppresses its cognate RelE toxin, we engineered C-terminal truncations of RelB and tested their functional effects on toxin suppression in E. coli. We find that removal of the long Cterminal a3 and connecting loop 4 (L4) of RelB prevents RelE suppression. Quantitative binding assays of RelE and RelB variants support a reduced affinity upon removal of the RelB C-terminus. Disrupting these interactions between RelB and RelE also led to a significant decrease in transcriptional repression at the relO operator, underscoring the requirement for RelE binding to RelB for optimal repression at DNA repressor elements. Comparison to other structurally homologous TA systems, such as E. coli DinJ-YafQ, reveals key differences in the molecular mechanisms of both toxin suppression and DNA repressor activity highlighting the diversity in TA regulation and function.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Escherichia Coli

SUBMITTER: Christine Dunham

LAB HEAD: Dunham, Christine

PROVIDER: PXD065338 | Pride | 2025-07-06

REPOSITORIES: Pride

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			Action	DRS
	20250418_IM_JT2.raw	Raw
	20250418_IM_JT2_peaks.dat	Other
	20250418_IM_JT4.raw	Raw
	20250418_IM_JT4_mzpeakdata.dat	Other

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