The multicopper oxidase (CueO) and cell aggregation in Escherichia coli

Jai J. Tree; Glenn C. Ulett; Jon L. Hobman; Chrystala Constantinidou; Nigel L. Brown; Christopher Kershaw; Mark A. Schembri; Michael P. Jennings; Alastair G. McEwan

doi:10.1111/j.1462-2920.2007.01320.x

The multicopper oxidase (CueO) and cell aggregation in Escherichia coli

Jai J. Tree, Glenn C. Ulett, Jon L. Hobman, Chrystala Constantinidou, Nigel L. Brown, Christopher Kershaw, Mark A. Schembri, Michael P. Jennings, Alastair G. McEwan

Research output: Contribution to journal › Article › peer-review

Abstract

cueO encodes a periplasmic multicopper oxidase, which is known to be involved in copper homeostasis and protection against oxidative stress in Escherichia coli K12. Transcriptional profiling showed that expression of genes associated with motility was lowered in a cueO mutant while expression of genes associated with autoaggregation was elevated. Increased aggregation was correlated with increased expression of cell surface proteins antigen 43 and curli. Changes in gene expression caused by the deletion of cueO were essentially independent of SoxR and OxyR, the global regulators of oxidative stress response. © 2007 The Authors.

Original language	English
Pages (from-to)	2110-2116
Number of pages	6
Journal	Environmental microbiology
Volume	9
Issue number	8
DOIs	https://doi.org/10.1111/j.1462-2920.2007.01320.x
Publication status	Published - Aug 2007

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title = "The multicopper oxidase (CueO) and cell aggregation in Escherichia coli",

abstract = "cueO encodes a periplasmic multicopper oxidase, which is known to be involved in copper homeostasis and protection against oxidative stress in Escherichia coli K12. Transcriptional profiling showed that expression of genes associated with motility was lowered in a cueO mutant while expression of genes associated with autoaggregation was elevated. Increased aggregation was correlated with increased expression of cell surface proteins antigen 43 and curli. Changes in gene expression caused by the deletion of cueO were essentially independent of SoxR and OxyR, the global regulators of oxidative stress response. {\textcopyright} 2007 The Authors.",

author = "Tree, {Jai J.} and Ulett, {Glenn C.} and Hobman, {Jon L.} and Chrystala Constantinidou and Brown, {Nigel L.} and Christopher Kershaw and Schembri, {Mark A.} and Jennings, {Michael P.} and McEwan, {Alastair G.}",

note = "Times Cited: 10",

year = "2007",

month = aug,

doi = "10.1111/j.1462-2920.2007.01320.x",

language = "English",

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pages = "2110--2116",

journal = "Environmental microbiology",

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T1 - The multicopper oxidase (CueO) and cell aggregation in Escherichia coli

AU - Tree, Jai J.

AU - Ulett, Glenn C.

AU - Hobman, Jon L.

AU - Constantinidou, Chrystala

AU - Brown, Nigel L.

AU - Kershaw, Christopher

AU - Schembri, Mark A.

AU - Jennings, Michael P.

AU - McEwan, Alastair G.

N1 - Times Cited: 10

PY - 2007/8

Y1 - 2007/8

N2 - cueO encodes a periplasmic multicopper oxidase, which is known to be involved in copper homeostasis and protection against oxidative stress in Escherichia coli K12. Transcriptional profiling showed that expression of genes associated with motility was lowered in a cueO mutant while expression of genes associated with autoaggregation was elevated. Increased aggregation was correlated with increased expression of cell surface proteins antigen 43 and curli. Changes in gene expression caused by the deletion of cueO were essentially independent of SoxR and OxyR, the global regulators of oxidative stress response. © 2007 The Authors.

AB - cueO encodes a periplasmic multicopper oxidase, which is known to be involved in copper homeostasis and protection against oxidative stress in Escherichia coli K12. Transcriptional profiling showed that expression of genes associated with motility was lowered in a cueO mutant while expression of genes associated with autoaggregation was elevated. Increased aggregation was correlated with increased expression of cell surface proteins antigen 43 and curli. Changes in gene expression caused by the deletion of cueO were essentially independent of SoxR and OxyR, the global regulators of oxidative stress response. © 2007 The Authors.

U2 - 10.1111/j.1462-2920.2007.01320.x

DO - 10.1111/j.1462-2920.2007.01320.x

M3 - Article

SN - 1462-2920

VL - 9

SP - 2110

EP - 2116

JO - Environmental microbiology

JF - Environmental microbiology

IS - 8

ER -

The multicopper oxidase (CueO) and cell aggregation in Escherichia coli

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