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4 results on '"Kallis, T."'

1. The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli

Author

Müller, Patrick, Ewers, C., Bertsche, U., Anstett, M., Kallis, T., Breukink, E.J., Fraipont, Claudine, Terrak, Mohammed, Nguyen-Distèche, Martine, Vollmer, W., Biochemistry of membranes, Membraan enzymologie, and Dep Scheikunde

Subjects
carbohydrates (lipids), bacteria
Abstract

Bacterial cell division requires the coordinated action of cell division proteins and murein (peptidoglycan) synthases. Interactions involving the essential cell division protein FtsN and murein synthases were studied by affinity chromatography with membrane fraction. The murein synthases PBP1A, PBP1B, and PBP3 had an affinity to immobilized FtsN. FtsN and PBP3, but not PBP1A, showed an affinity to immobilized PBP1B. The direct interaction between FtsN and PBP1B was confirmed by pulldown experiments and surface plasmon resonance. The interaction was also detected by bacterial two-hybrid analysis. FtsN and PBP1B could be cross-linked in intact cells of the wild type and in cells depleted of PBP3 or FtsW. FtsN stimulated the in vitro murein synthesis activities of PBP1B. Thus, FtsN could have a role in controlling or modulating the activity of PBP1B during cell division in Escherichia coli.

Published
2007

2. The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli

Author

Biochemistry of membranes, Membraan enzymologie, Dep Scheikunde, Müller, Patrick, Ewers, C., Bertsche, U., Anstett, M., Kallis, T., Breukink, E.J., Fraipont, Claudine, Terrak, Mohammed, Nguyen-Distèche, Martine, Vollmer, W., Biochemistry of membranes, Membraan enzymologie, Dep Scheikunde, Müller, Patrick, Ewers, C., Bertsche, U., Anstett, M., Kallis, T., Breukink, E.J., Fraipont, Claudine, Terrak, Mohammed, Nguyen-Distèche, Martine, and Vollmer, W.

Published
2007

4. The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli.

Author

Müller P, Ewers C, Bertsche U, Anstett M, Kallis T, Breukink E, Fraipont C, Terrak M, Nguyen-Distèche M, and Vollmer W

Subjects
Chromatography, Affinity, Escherichia coli chemistry, Escherichia coli Proteins chemistry, Membrane Proteins chemistry, Penicillin-Binding Proteins chemistry, Peptidoglycan Glycosyltransferase chemistry, Protein Binding physiology, Serine-Type D-Ala-D-Ala Carboxypeptidase chemistry, Surface Plasmon Resonance, Two-Hybrid System Techniques, Cell Division physiology, Escherichia coli physiology, Escherichia coli Proteins metabolism, Membrane Proteins metabolism, Penicillin-Binding Proteins metabolism, Peptidoglycan Glycosyltransferase metabolism, Serine-Type D-Ala-D-Ala Carboxypeptidase metabolism
Abstract

Bacterial cell division requires the coordinated action of cell division proteins and murein (peptidoglycan) synthases. Interactions involving the essential cell division protein FtsN and murein synthases were studied by affinity chromatography with membrane fraction. The murein synthases PBP1A, PBP1B, and PBP3 had an affinity to immobilized FtsN. FtsN and PBP3, but not PBP1A, showed an affinity to immobilized PBP1B. The direct interaction between FtsN and PBP1B was confirmed by pulldown experiments and surface plasmon resonance. The interaction was also detected by bacterial two-hybrid analysis. FtsN and PBP1B could be cross-linked in intact cells of the wild type and in cells depleted of PBP3 or FtsW. FtsN stimulated the in vitro murein synthesis activities of PBP1B. Thus, FtsN could have a role in controlling or modulating the activity of PBP1B during cell division in Escherichia coli.

Published
2007
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