Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.641862
Title: Studies on the ftsW and mraY genes of Escherichia coli
Author: Boyle, David S.
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1995
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Abstract:
The morphogenes are genes required for cell growth and division in Escherichia coli. The morphogenes are often grouped as clusters in different regions of the chromosome. The mra region, located at 2 minutes on the E. coli chromosome is the largest cluster of morphogenes. It contains sixteen open reading frames from which fourteen genes have been identified as encoding for proteins involved in either cell division or the biosynthesis of the cell wall. The organisation of the cluster appears to be complex with the genes tightly packed and often overlapping. Many of the genes appear to share promoters for their expression. However, several of these genes have been incompletely characterized. The predicted proteins encoded by ftsW, a cell division gene, and mraY, a gene required for murein synthesis, have not yet been identified. One of the aims of this study was to identify the peptides produced from ftsW an mraY. The mutant phenotypes of these genes are poorly characterized. At the time of this study there was no temperature sensitive ftsW allele and there was no mutant allele of mraY. In this study null mutants were made for both ftsW and mraY. This allowed a more accurate characterization of their roles in cell division and cell growth, respectively. The isolation of the mutants allowed studies on their complementation. The promoter regions required for the independent expression of ftsW and mraY were then identified. The close proximity of genes in the mra region, the presence of overlaps and the sharing of promoters has provoked speculation that several of these genes may be translationally coupled. A previous study on three genes of the mra cluster revealed no translational coupling between the three genes but showed differences in the efficiency of translation of each gene product.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.641862  DOI: Not available
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