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The multicopper oxidase (CueO) and cell aggregation in Escherichia coli
Author(s) -
Tree Jai J.,
Ulett Glenn C.,
Hobman Jon L.,
Constantinidou Chrystala,
Brown Nigel L.,
Kershaw Christopher,
Schembri Mark A.,
Jennings Michael P.,
McEwan Alastair G.
Publication year - 2007
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/j.1462-2920.2007.01320.x
Subject(s) - periplasmic space , biology , escherichia coli , multicopper oxidase , microbiology and biotechnology , gene , mutant , escherichia coli proteins , oxidative stress , cell , gene expression , biochemistry , enzyme , laccase
Summary 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.