PMID:9226273

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Citation

Pichoff, S, Vollrath, B and Bouché, JP (1997) MinCD-independent inhibition of cell division by a protein that fuses MalE to the topological specificity factor MinE. J. Bacteriol. 179:4616-9

Abstract

We report that MinE, the topological specificity factor of cell division in Escherichia coli, inhibits septation when fused to the C terminus of the maltose-binding protein MalE. This contrasts with overexpression of MinE alone, which affects growth but has no effect on division. Inhibition by MalE-MinE was minCD independent and depended on MinE segments involved in dimerization and prevention of MinCD division inhibition. The SOS and the heat shock responses were not involved, suggesting that the inhibition comes from a direct interaction of MalE-MinE with the septation apparatus. MalE-MinE lethality was suppressed by overexpression of ftsZ, as well as by overexpression of ftsN, a suppressor of temperature-sensitive mutations in genes ftsQ, ftsA, and ftsI. We also report that high-level synthesis of MalE disturbs nucleoid partitioning.

Links

PubMed PMC179299

Keywords

ATP-Binding Cassette Transporters; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carrier Proteins/genetics; Carrier Proteins/metabolism; Cell Cycle Proteins; Cell Division; Cytoskeletal Proteins; Escherichia coli/cytology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Heat-Shock Response; Maltose-Binding Proteins; Membrane Proteins/genetics; Monosaccharide Transport Proteins; Periplasmic Binding Proteins; Recombinant Fusion Proteins/metabolism; SOS Response (Genetics); Sequence Deletion; Suppression, Genetic

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