Tanneke Den Blaauwen

Publication Date: 2003

Publication Name: Molecular Microbiology

Research Interests:
Molecular Microbiology, Polymers, Cytoskeleton, Cell Division, Biological Sciences, and 8 moreSequence alignment, Escherichia coli, Temperature, Trypsin, Arginine, Amino Acid Sequence, Molecular Sequence Data, and Cell Membrane

Download (.pdf)

Publication Date: 2008

Publication Name: Molecular Microbiology

Research Interests:
Membrane Proteins, Molecular Microbiology, Macromolecular X-Ray Crystallography, Cell Division, Biological Sciences, and 9 moreMolecular, Crystal structure, Mutation, Escherichia coli, Protein Secondary Structure Prediction, Cell Wall, Site-directed Mutagenesis, Dimerization, and Yersinia Enterocolitica

Download ()

Publication Date: 1999

Publication Name: FEBS Letters

Research Interests:
Thermodynamics, Differential scanning calorimetry, Membrane transport proteins, Heat Capacity, Bacillus subtilis, and 6 moreIsothermal Titration Calorimetry, Protein Conformation, Nucleotides, Biochemistry and cell biology, Adenosine Triphosphate, and Adenosine Diphosphate

Download (.pdf)

Publication Date: 2013

Publication Name: Journal of Biological Chemistry

Research Interests:
Membrane Proteins, Biological Chemistry, Cell Division, Biological Sciences, Escherichia coli, and 3 moreCHEMICAL SCIENCES, Protein Quaternary Structure, and Cell Cycle Proteins

Download (.pdf)

Cell division in E. coli involves a set of essential proteins that assembles at midcell to form the so-called divisome. The divisome regulates the invagination of the inner membrane, cell wall synthesis and inward growth of the outer... more

Cell division in E. coli involves a set of essential proteins that assembles at midcell to form the so-called divisome. The divisome regulates the invagination of the inner membrane, cell wall synthesis and inward growth of the outer membrane. One of the divisome proteins, FtsQ, plays a central but enigmatic role in cell division. This protein associates with FtsB and FtsL, which, like FtsQ, are bitopic inner membrane proteins with a large periplasmic domain (denoted FtsQp, FtsBp and FtsLp) that is indispensible for the function of each protein. Considering the vital nature and accessible location of the FtsQBL complex, it is an attractive target for protein-protein interaction (PPI) inhibitors intended to block bacterial cell division. In this study, we expressed FtsQp, FtsBp and FtsLp individually and in combination. Upon co-expression, FtsQp was co-purified with FtsBp and FtsLp from E. coli extracts as a stable trimeric complex. FtsBp was also shown to interact with FtsQp in the ...

Publication Date: Jan 9, 2015

Publication Name: The Journal of biological chemistry

Research Interests:
Biological Chemistry, Biological Sciences, and CHEMICAL SCIENCES

Publication Date: 2007

Publication Name: Annual Review of Microbiology

Research Interests:
Microbiology, Medical Microbiology, Energy Metabolism, Bacteria, and Protein Biosynthesis

Download (.pdf)

Publication Date: 2007

Publication Name: Microbiology and Molecular Biology Reviews

Research Interests:
Microbiology, Technology, Cell Cycle, DNA replication, DNA repair, and 6 moreBiological Sciences, Bacteria, Flagella, Health Science, Structural Complexity, and Gene Expression Regulation

Download (.pdf)

The increase in antibiotic resistant bacteria demands the development of new antibiotics against preferably new targets. The common approach is to test compounds for their ability to kill bacteria or to design molecules that inhibit... more

The increase in antibiotic resistant bacteria demands the development of new antibiotics against preferably new targets. The common approach is to test compounds for their ability to kill bacteria or to design molecules that inhibit essential protein activities in vitro. In the first case, the mode of action of the drug is unknown and in the second case, it is not known whether the compound will pass the impermeable barrier of the bacterial envelope. We developed an assay that detects the target of a compound, as well as its ability to pass the membrane(s) simultaneously. The Escherichia coli cytoskeletal protein MreB recruits protein complexes (elongasomes) that are essential for cell envelope growth. An in cell Förster Resonance Energy Transfer (FRET) assay was developed to detect the interaction between MreB molecules and between MreB and the elongasome proteins RodZ, RodA and PBP2. Inhibition of the polymerization of MreB by S-(3,4-dichlorobenzyl) isothiourea (A22) or of the activity of PBP2 by mecilinam resulted in loss or reduction of all measured interactions. This suggests that the interactions between the elongasome proteins are governed by a combination of weak affinities and substrate availability. This validated in cell FRET assay can be used to screen for cell envelope growth inhibitors.