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Published on: May 31, 2024
Structure and activity of AbiQ, a lactococcal endoribonuclease belonging to the type III toxin-antitoxin system
Julie E Samson1, Silvia Spinelli, Christian Cambillau
1Département de biochimie, de microbiologie et de bio-informatique, Faculté des sciences et génie, Université Laval, Québec, Canada, G1V 0A6.
Abstract:
AbiQ is a phage resistance mechanism found on a native plasmid of Lactococcus lactis that abort virulent phage infections. In this study, we experimentally demonstrate that AbiQ belongs to the recently described type III toxin-antitoxin systems. When overexpressed, the AbiQ protein (ABIQ) is toxic and causes bacterial death in a bacteriostatic manner. Northern and Western blot experiments revealed that the abiQ gene is transcribed and translated constitutively, and its expression is not activated by a phage product. ABIQ is an endoribonuclease that specifically cleaves its cognate antitoxin RNA molecule in vivo. The crystal structure of ABIQ was solved and site-directed mutagenesis identified key amino acids for its anti-phage and/or its RNase function. The AbiQ system is the first lactococcal abortive infection system characterized to date at a structural level.
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