Inactivation of Terminal Oxidase bd-I Leads to Supersensitivity of E. coli to Quinolone and Beta-Lactam Antibiotics

• Published in: Molecular biology (New York) Vol. 56; no. 4; pp. 572 - 579
• Main Authors: Seregina, T. A., Lobanov, K. V., Shakulov, R. S., Mironov, A. S.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.08.2022; Springer Nature B.V
• Subjects: 3-Mercaptopyruvate sulfurtransferase; Antibiotics; Biochemistry; Biomedical and Life Sciences; Chromosomes; Cytochrome; Cytochrome bd; E coli; Escherichia coli; Genomes; Human Genetics; Hydrogen sulfide; Hydroquinone; Life Sciences; Molecular Cell Biology; Oxidative stress; Sulfurtransferase; Terminal oxidase; β-Lactam antibiotics; terminal oxidase bd-I; hydrogen sulfide; deletions; and; catalase KatG; oxidative stress; supersensitivity to antibiotics
• ISSN: 0026-8933; 1608-3245
• DOI: 10.1134/S0026893322040100

In cells of Escherichia coli , terminal oxidase bd-I encoded by the cydAB gene catalyzes the reduction of O 2 to water using hydroquinone as an electron donor. In addition to the cydAB operon, two other genes, cydC and cydD , encoding the heterodimeric ATP-binding cassette-type transporter are essential for the assembly of cytochrome bd-I. It was shown that inactivation of cytochrome bd-I by the introduction of cydB or cydD deletions into the E. coli chromosome leads to supersensitivity of the bacteria to antibiotics of the quinolone and beta-lactam classes. The sensitivity of these mutants to antibiotics is partially suppressed by introduction of a constitutively expressed gene katG under the control of the P tet promoter into their genome. The increased level of hydrogen sulfide resulting from the introduction of the mstA gene, encoding 3-mercaptopyruvate sulfurtransferase, under the control of the P tet promoter, leads to the same effect. These data demonstrate the important role of cytochrome bd-I in the defense of bacteria from oxidative stress and bactericidal antibiotics.