Dirk-Jan Scheffers

GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers.

Immediate GTP hydrolysis upon FtsZ polymerization.

Cytokinesis in bacteria.

R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division.

Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis.

PBP1 is a component of the Bacillus subtilis cell division machinery.

Dynamic localization of penicillin-binding proteins during spore development in Bacillus subtilis.

Bacterial cell wall synthesis: new insights from localization studies.

Cell wall growth during elongation and division: one ring to bind them?

Contribution of the FtsQ transmembrane segment to localization to the cell division site.

Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis.

The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA.

YidC is required for the assembly of the MscL homopentameric pore.

Diffusion nuclear magnetic resonance spectroscopy detects substoichiometric concentrations of small molecules in protein samples.

Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.

Activators of the glutamate-dependent acid resistance system alleviate deleterious effects of YidC depletion in Escherichia coli.

Large ring polymers align FtsZ polymers for normal septum formation.

Bacillus subtilis SepF binds to the C-terminus of FtsZ.

Balanced transcription of cell division genes in Bacillus subtilis as revealed by single cell analysis.

Phage 29 phi protein p1 promotes replication by associating with the FtsZ ring of the divisome in Bacillus subtilis.

The localization of key Bacillus subtilis penicillin binding proteins during cell growth is determined by substrate availability.

Focus on membrane differentiation and membrane domains in the prokaryotic cell.