Journal
JOURNAL OF BACTERIOLOGY
Volume 189, Issue 2, Pages 646-649Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00992-06
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Funding
- NIGMS NIH HHS [GM38922, R01 GM038922] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM038922, R37GM038922] Funding Source: NIH RePORTER
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FtsN, the last essential protein in the cell division localization hierarchy in Escherichia coli, has several peculiar characteristics, suggesting that it has a unique role in the division process despite the fact that it is conserved in only a subset of bacteria. In addition to suppressing temperature-sensitive mutations in ftsA, ftsK, ftsQ, and ftsI, overexpression of FtsN can compensate for a complete lack of FtsK in the cell. We examined the requirements for this phenomenon. We found that the N-terminal terminal region (cytoplasmic and transmembrane domains) is critical for suppression, while the C-terminal murein-binding domain is dispensable. Our results further suggest that FtsN and FtsK act cooperatively to stabilize the divisome.
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