Article Abstract:
FtsZ is a soluble, tubulin-like GTPase that produces a membrane-associated ring at the division site of bacterial cells. FtsZ was found to bind directly to a unique integral inner-membrane protein in Escherichia coli which is designated as ZipA. Genetic and morphological evidence show that this interaction is needed for cells division. Also, a fluorescent ZipA-Gfp fusion protein is situated in a ring structure at the division site. Therefore, ZipA is a crucial component of the division mechanism and may be directly involved in the assembly and/or function of the FtsZ ring.
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Article Abstract:
The rpoS is a stationary-phase induced gene acting as regulator that is essential to gene expression during feast-to-famine transition in Escherichia coli. This regulator is strongly homologous to the vegetative sigma factor, indicating that it acts as an alternative sigma subunit of RNA polymerase. Several rpoS-dependent genes and their corresponding cellular functions have also been identified. In addition, related studies implicate the rpoS gene as an osmoregulatory gene.
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Article Abstract:
Research was conducted to determine the gene expression in cultures of Escherichia coli in situ and online via an electrochemical sensor. The transcriptional fusion of lacZ to the RpoS-dependent osmY gene was used to monitor the online progress of E. coli into stationary phase. Results indicate that the method used will be useful in determining the activity of any promoter with a variety of reporter genes.
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