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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
50
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pubmed:dateCreated |
2007-12-10
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36394-402
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pubmed:meshHeading |
pubmed-meshheading:17938168-Cell Division,
pubmed-meshheading:17938168-Chromatography, Affinity,
pubmed-meshheading:17938168-Escherichia coli,
pubmed-meshheading:17938168-Escherichia coli Proteins,
pubmed-meshheading:17938168-Membrane Proteins,
pubmed-meshheading:17938168-Penicillin-Binding Proteins,
pubmed-meshheading:17938168-Peptidoglycan Glycosyltransferase,
pubmed-meshheading:17938168-Protein Binding,
pubmed-meshheading:17938168-Serine-Type D-Ala-D-Ala Carboxypeptidase,
pubmed-meshheading:17938168-Surface Plasmon Resonance,
pubmed-meshheading:17938168-Two-Hybrid System Techniques
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pubmed:year |
2007
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pubmed:articleTitle |
The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli.
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pubmed:affiliation |
Microbial Genetics, University of Tübingen, 72076 Tübingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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