Blencowe, Dayle, al Jubori, Sawsan and Morby, Andrew P. 2011. Identification of a novel function for the FtsL cell division protein from Escherichia coli K12. Biochemical and Biophysical Research Communications 411 (1) , pp. 44-49. 10.1016/j.bbrc.2011.06.083 |
Abstract
Analysis of the essential cell division protein FtsL demonstrates the partial conservation of a cysteine-pair within the trans-membrane region which itself is flanked by histidine-pairs in the cytosol and periplasm. Similar arrangements of such amino acids are seen in proteins known to transport/bind metal ions in biological systems. Heterologous expression of ftsL in Escherichia coli K12 confers a Zn(II)-sensitive phenotype and alteration of the candidate metal-ion binding residues cysteine or histidine substantially alters this phenotype. Whilst the cysteine/histidine replacement derivatives of ftsL were able to complement an otherwise ftsL-null strain, the derivative carrying ftsL lacking the cysteine pair was sensitive to raised metal-ion concentrations in the media. We show that ftsL can confer a metal-ion sensitive phenotype and that trans-membrane cysteine residues play a role in FtsL function in elevated metal-ion concentrations.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Biosciences |
Subjects: | Q Science > Q Science (General) |
Uncontrolled Keywords: | Zn(II); cell-division; FtsL |
Publisher: | Elsevier |
ISSN: | 0006-291X |
Last Modified: | 04 Jun 2017 03:16 |
URI: | https://orca.cardiff.ac.uk/id/eprint/19045 |
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