Thomas G. Bernhardt

The paper identifies gain-of-function mutations in RodZ that enhance Rod system activity in E. coli by mimicking FtsN's role in divisome activation.

This study investigates MOMP assembly in Corynebacterium glutamicum, showing that PorH and ProtX are inserted at polar growth zones and linked to the cell wall.

This paper identifies the TmaT-AftD interaction as essential for mycolate transport via the CmpL4 pathway and AG synthesis in Corynebacterium glutamicum.

This paper identifies LysZ as a phage gene required for lysis of Corynebacterium glutamicum, showing that phages overcome mycomembrane barriers by targeting membrane-anchored glycopolymers.

The paper identifies PlsX as a suppressor of cell elongation defects in E. coli, suggesting acyl-phosphate regulates LPS synthesis by inhibiting LpxC.

The paper determines the structure of MreC-MreD complex and shows how MreD controls MreC conformation, essential for bacterial cell shape and antibiotic targeting.

This study shows that MreB couples the cell wall to the cytoplasmic membrane in E. coli, increasing resistance to bending and preventing membrane detachment under stress.

This study shows LpoB transiently binds and activates PBP1b through an allosteric switch, directing PG synthesis to low-density areas and enabling lipoprotein redistribution.

This study identifies PBP1b's specialized role in E. coli division site fortification against osmotic rupture, showing it functions independently of LpoB and requires an extended N-terminus for recruitment by FtsA.

This study identifies the σD envelope stress response in Corynebacterium glutamicum as critical for monitoring mycolic acid and arabinogalactan biosynthesis defects, revealing its role in envelope integrity maintenance.

The paper identifies an activation pathway involving PBP2 that enhances cell wall polymerization and MreB filament formation in E. coli.

The paper shows that LDT-mediated crosslinks in mycobacteria are crucial for maintaining rod shape at aging cell wall sites, and their absence makes Mtb more susceptible to combined PBP and LDT-inhibiting drugs.

The paper investigates how MOP-family flippases recognize and transport lipid-linked oligosaccharides, finding that substrate binding destabilizes the inward-open conformation to promote translocation.