Type II toxin-antitoxin (TA) systems encode two proteins: a toxin that inhibits cell growth and an antitoxin that neutralizes the toxin by direct inter-molecular protein-protein inter-actions. The bacterial HipBA TA system is implicated in persister formation. The HipBA TA system consists of a HipB antitoxin and a HipA toxin, the latter of which is split into two fragments, and here we investigate this novel three-com-ponent regulatory HipBA system. Structural and functional analysis revealed that HipA corresponds to the N-ter-minal part of HipA from other bacteria and toxic HipA is inactivated by HipA, not HipB. This study will be helpful in understanding the detailed regulatory mechanism of the HipBA system, as well as why it is constructed as a three-com-ponent system.
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| http://dx.doi.org/10.1107/S205225252200687X | DOI Listing |
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Article Synopsis
- - Toxin-antitoxin (TA) systems are essential genetic structures found in bacteria and archaea, and the study focuses on the Legionella pneumophila effector Lpg2370, identifying it as a Ser/Thr kinase.
- - Lpg2370 functions within the HipBST TA system, alongside two upstream genes, with its toxin (Lpg2370) and antitoxin (Lpg2369) being related to the HipA protein in a different TA system.
- - Structural analysis of Lpg2370 reveals critical residues for ATP binding and shows that its interaction with the antitoxin Lpg2369 inhibits its kinase activity, providing insights into how the HipBST TA system operates.
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