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Abstract

The gene from HB8 encodes an orthologue of the copper-sensing transcriptional repressor CsoR. X-ray crystal structure analysis of . CsoR indicated that it forms a homotetramer. The structures of the CsoR monomer and dimer are similar to those of CsoR. In the absence of copper ions, . CsoR bound to the promoter region of the copper-sensitive operon --, which encodes the copper chaperone CopZ, CsoR and the copper efflux P-type ATPase CopA, to repress their expression, while in the presence of approximately an equal amount of copper ion, CsoR was released from the DNA, to allow expression of the downstream genes. Both Cu(II) and Cu(I) ions could bind CsoR, and were effective for transcriptional derepression. Additionally, CsoR could also sense various other metal ions, such as Zn(II), Ag(I), Cd(II) and Ni(II), which led to transcriptional derepression. The copper-binding motif of . CsoR contains C-H-H, while those of most orthologues contain C-H-C. The X-ray crystal structure of . CsoR suggests that a histidine residue in the N-terminal domain is also involved in metal-ion binding; that is, the binding motif could be H-C-H-H, like that of RcnR, which binds Ni(II)/Co(II). The non-conserved H70 residue in the metal-binding motif of . CsoR is important for its DNA-binding affinity and metal-ion responsiveness.

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2010-07-01
2019-10-15
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Oligonucleotides used in this study [PDF](13 KB)

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Gel-filtration analysis of the wild-type and H70C mutant CsoR proteins [PDF](118 KB)

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