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Review
. 2024:104:17-31.
doi: 10.1007/978-3-031-58843-3_2.

The Copper Efflux Regulator (CueR)

Affiliations
Review

The Copper Efflux Regulator (CueR)

Yangbo Hu et al. Subcell Biochem. 2024.

Abstract

The copper efflux regulator (CueR) is a classical member of the MerR family of metalloregulators and is common in gram-negative bacteria. Through its C-terminal effector-binding domain, CueR senses cytoplasmic copper ions to regulate the transcription of genes contributing to copper homeostasis, an essential process for survival of all cells. In this chapter, we review the regulatory roles of CueR in the model organism Escherichia coli and the mechanisms for CueR in copper binding, DNA recognition, and interplay with RNA polymerase in regulating transcription. In light of biochemical and structural analyses, we provide molecular details for how CueR represses transcription in the absence of copper ions, how copper ions mediate CueR conformational change to form holo CueR, and how CueR bends and twists promoter DNA to activate transcription. We also characterize the functional domains and key residues involved in these processes. Since CueR is a representative member of the MerR family, elucidating its regulatory mechanisms could help to understand the CueR-like regulators in other organisms and facilitate the understanding of other metalloregulators in the same family.

Keywords: Allosteric activation; Copper homeostasis; Metalloregulator; Promoter; RNA polymerase; Transcriptional regulation.

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References

    1. Andoy NM, Sarkar SK, Wang Q, Panda D, Benitez JJ, Kalininskiy A, Chen P (2009) Single-molecule study of metalloregulator CueR-DNA interactions using engineered Holliday junctions. Biophys J 97(3):844–852. https://doi.org/10.1016/j.bpj.2009.05.027 - DOI - PubMed - PMC
    1. Andrei A, Ozturk Y, Khalfaoui-Hassani B, Rauch J, Marckmann D, Trasnea PI, Daldal F, Koch HG (2020) Cu homeostasis in bacteria: the ins and outs. Membranes (Basel) 10(9). https://doi.org/10.3390/membranes10090242
    1. Ansari AZ, Bradner JE, O'Halloran TV (1995) DNA-bend modulation in a repressor-to-activator switching mechanism. Nature 374(6520):371–375. https://doi.org/10.1038/374370a0 - DOI - PubMed
    1. Balogh RK, Gyurcsik B, Hunyadi-Gulyas E, Schell J, Thulstrup PW, Hemmingsen L, Jancso A (2019) C-terminal cysteines of CueR act as auxiliary metal site ligands upon hg(II) binding-a mechanism to prevent transcriptional activation by divalent metal ions? Chemistry 25(66):15030–15035. https://doi.org/10.1002/chem.201902940 - DOI - PubMed - PMC
    1. Balogh RK, Gyurcsik B, Jensen M, Thulstrup PW, Koster U, Christensen NJ, Jensen ML, Hunyadi-Gulyas E, Hemmingsen L, Jancso A (2022) Tying up a loose end: on the role of the C-terminal CCHHRAG fragment of the Metalloregulator CueR. Chembiochem 23(16):e202200290. https://doi.org/10.1002/cbic.202200290 - DOI - PubMed - PMC

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