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. 2018 Nov 29;47(2):843–854. doi: 10.1093/nar/gky1201

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 1. — The ACT domain is required for the interaction between SpoT and EIIA^Ntr∼P in a bacterial two-hybrid assay. (A) Domain organisation of C. crescentus SpoT with the catalytic domains, HD and SD, located at the N-terminal extremity and the regulatory domains, TGS and ACT, located at the C-terminal end. The SpoT variants used in the BTH assay (SpoT_Δ668–719 and ACT_506–742) are also represented. (B) SpoT and ACT_506–742, but not SpoT_Δ668–719, directly interact with EIIA^Ntr∼P. β-galactosidase assays were performed on MG1655 cyaA::frt (RH785) strains coexpressing T18- fused to ptsN, spoT, spoT_Δ_668–719 or ACT_506–742 with T25- fused to ptsN, spoT or spoT_Δ_668–719. Error bars = SD, n = 3.