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Britta Girbardt

As seen in: Nature
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Articles

Reprogramming of bacterial virulence by lysine acetylation

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By Ole Schmöker, Britta Girbardt, Sabrina Schulze, Gottfried J. Palm, Leona Berndt, Nilufer Kara, Ruba Al-Abdulla, Heike Junker, Leif Steil, Christian Hentschker, Vanessa Lachmayer, Mark Dorr, Stefan Kemnitz, Stefan Müller, Jan-Wilm Lackmann, Marcus Kruger, Kay H Hofmann, Uwe T. Bornscheuer, Uwe Völker, Elke Krüger, Vera Kozjak-Pavlovic, Michael Lammers, Jens Hoppen, Xenia Schöps, Klara Garz, Sophie Wolfgramm, Katrin Schoknecht, Lea-Maria Mayer, Leonie Speth
| Nature Verified
Abstract Gram-negative bacteria use a plethora of virulence factors to infect eukaryotic cells. CE-clan protease-related virulence factors were reported to act as deubiquitinases/ubiquitin-like specific proteases. Some have an additional acetyl-transferase activity. The molecular mechanisms underlying this dual activity and the physiological consequences are only marginally understood.
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AcuB senses cellular energy charge to coordinate acetyl-CoA synthesis in bacteria

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By Norman Geist, Sabrina Schulze, Gottfried J. Palm, Leona Berndt, Daniel Weis, Norma Welsch, Thomas Schweder, Mark Dorr, Stefan Kemnitz, Uwe T. Bornscheuer, Mihaela Delcea, Michael Lammers, Markus Janetzky, Henriette Rückert, Kimani Gatzemeyer, Britta Girbardt, Ina Menyes
| Nature Verified
Abstract Bacteria adjust their metabolism to the cellular energy state. AMP-forming acetyl-CoA-synthetase AcsA generates acetyl-CoA from acetate, ATP and CoA. In Bacilli, including Bacillus subtilis and Geobacillus stearothermophilus, AcsA is reversely transcribed upstream of the acu-operon encoding for the proteins AcuA, AcuB and AcuC. Lysine-acetyltransferase AcuA uses acetyl-CoA to acetylate and inactivate AcsA, while AcuC re-activates AcsA activity by deacetylation.
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