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Trigger factor depletion or overproduction causes defective cell division but does not block protein export
1Molecular Biology Institute, University of California, Los Angeles 90024-1737.
Journal of Bacteriology
|October 1, 1990
Summary
Escherichia coli trigger factor protein does not affect proOmpA secretion but is crucial for cell division. Depletion or overproduction of trigger factor leads to cell filamentation, indicating its essential role in bacterial cell cycle regulation.
Area of Science:
- Microbiology
- Molecular Biology
- Cell Biology
Background:
- Trigger factor is a cytosolic protein in Escherichia coli.
- It stabilizes proOmpA for translocation across inner membranes in vitro.
- Its precise physiological role in vivo remains to be fully elucidated.
Purpose of the Study:
- To investigate the in vivo function of trigger factor in Escherichia coli.
- To determine the effect of trigger factor levels on protein secretion and cell division.
- To understand the physiological consequences of trigger factor depletion or overproduction.
Main Methods:
- Isolation and sequencing of the trigger factor gene.
- Construction of Escherichia coli strains with regulated trigger factor expression.
- Analysis of proOmpA synthesis and secretion rates in depleted cells.
- Observation of cell morphology in trigger factor-depleted and overproducing strains.
- Genetic analysis using multicopy plasmids, including ftsZ.
Main Results:
- No defect in in vivo proOmpA synthesis or secretion was observed in trigger factor-depleted cells.
- Trigger factor depletion or overproduction resulted in an enrichment of filamented cells.
- Filamentation in trigger factor-overproducing cells was suppressed by expressing the ftsZ gene.
Conclusions:
- Trigger factor is not essential for proOmpA secretion in vivo.
- Trigger factor plays a significant role in Escherichia coli cell division.
- The ftsZ gene, essential for cell division, can suppress trigger factor-related filamentation.