Sabrina Schulze

Nov 3, 2024 | nature.com | Carlos Moreno-Yruela |Sabrina Schulze |Gottfried J. Palm |Nancy Wang |Dianna Hocking |Leila Jebeli | +5 more

AbstractClassical Zn2+-dependent deac(et)ylases play fundamental regulatory roles in life and are well characterized in eukaryotes regarding their structures, substrates and physiological roles. In bacteria, however, classical deacylases are less well understood. We construct a Generalized Profile (GP) and identify thousands of uncharacterized classical deacylases in bacteria, which are grouped into five clusters.

Nov 3, 2024 | nature.com | Carlos Moreno-Yruela |Sabrina Schulze |Gottfried J. Palm |Nancy Wang |Dianna Hocking |Leila Jebeli | +5 more

AbstractClassical Zn2+-dependent deac(et)ylases play fundamental regulatory roles in life and are well characterized in eukaryotes regarding their structures, substrates and physiological roles. In bacteria, however, classical deacylases are less well understood. We construct a Generalized Profile (GP) and identify thousands of uncharacterized classical deacylases in bacteria, which are grouped into five clusters.

Feb 22, 2024 | nature.com | Sabrina Schulze |Gottfried J. Palm |Susanne Sievers |Ulrich Baumann |Karin Schnetz

AbstractThe Escherichia coli TetR-related transcriptional regulator RutR is involved in the coordination of pyrimidine and purine metabolism. Here we report that lysine acetylation modulates RutR function. Applying the genetic code expansion concept, we produced site-specifically lysine-acetylated RutR proteins. The crystal structure of lysine-acetylated RutR reveals how acetylation switches off RutR-DNA-binding. We apply the genetic code expansion concept in E.