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A novel sensor of NADH/NAD+ redox poise in Streptomyces coelicolor A3(2)

journal contribution
posted on 2023-06-08, 06:17 authored by Dimitris Brekasis, Mark PagetMark Paget
We describe the identification of Rex, a novel redox-sensing repressor that appears to be widespread among Gram-positive bacteria. In Streptomyces coelicolor Rex binds to operator (ROP) sites located upstream of several respiratory genes, including the cydABCD and rex-hemACD operons. The DNA-binding activity of Rex appears to be controlled by the redox poise of the NADH/NAD+ pool. Using electromobility shift and surface plasmon resonance assays we show that NADH, but not NAD+, inhibits the DNA-binding activity of Rex. However, NAD+ competes with NADH for Rex binding, allowing Rex to sense redox poise over a range of NAD(H) concentrations. Rex is predicted to include a pyridine nucleotide-binding domain (Rossmann fold), and residues that might play key structural and nucleotide binding roles are highly conserved. In support of this, the central glycine in the signature motif (GlyXGlyXXGly) is shown to be essential for redox sensing. Rex homologues exist in most Gram-positive bacteria, including human pathogens such as Staphylococcus aureus, Listeria monocytogenes and Streptococcus pneumoniae.

History

Publication status

  • Published

Journal

EMBO Journal

ISSN

0261-4189

Publisher

Nature Publishing Group

Issue

18

Volume

22

Page range

4856-4865

Pages

10.0

Department affiliated with

  • Biochemistry Publications

Notes

Brekasis was a PhD student in Paget's lab when the work was conceived, carried out and written up. Brekasis performed all practical aspects under Paget's supervision and Paget wrote up the manuscript. The work describes for the first time a sensor of NADH/NAD+ redox poise in bacteria.

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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