Home > Publications database > Identification of Gip as a novel phage‐encoded gyrase inhibitor protein of Corynebacterium glutamicum > print

001     897245
005     20230303093547.0
024 7 _ |a 10.1111/mmi.14813
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024 7 _ |a 1365-2958
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100 1 _ |a Kever, Larissa
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245 _ _ |a Identification of Gip as a novel phage‐encoded gyrase inhibitor protein of Corynebacterium glutamicum
260 _ _ |a Oxford [u.a.]
|c 2021
|b Wiley-Blackwell
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500 _ _ |a Biotechnologie 1
520 _ _ |a By targeting key regulatory hubs of their host, bacteriophages represent a powerful source for the identification of novel antimicrobial proteins. Here, a screening of small cytoplasmic proteins encoded by the CGP3 prophage of Corynebacterium glutamicum resulted in the identification of the gyrase-inhibiting protein Cg1978, termed Gip. Pull-down assays and surface plasmon resonance revealed a direct interaction of Gip with the gyrase subunit A (GyrA). The inhibitory activity of Gip was shown to be specific to the DNA gyrase of its bacterial host C. glutamicum. Overproduction of Gip in C. glutamicum resulted in a severe growth defect as well as an induction of the SOS response. Furthermore, reporter assays revealed an RecA-independent induction of the cryptic CGP3 prophage, most likely caused by topological alterations. Overexpression of gip was counteracted by an increased expression of gyrAB and a reduction of topA expression at the same time, reflecting the homeostatic control of DNA topology. We postulate that the prophage-encoded Gip protein plays a role in modulating gyrase activity to enable efficient phage DNA replication. A detailed elucidation of the mechanism of action will provide novel directions for the design of drugs targeting DNA gyrase.
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700 1 _ |a Hünnefeld, Max
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700 1 _ |a Brehm, Jannis
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700 1 _ |a Heermann, Ralf
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700 1 _ |a Frunzke, Julia
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|e Corresponding author
773 _ _ |a 10.1111/mmi.14813
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|t Molecular microbiology
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|y 2021
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856 4 _ |u https://juser.fz-juelich.de/record/897245/files/mmi.14813.pdf
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