Nik Operon

The ''nik operon'' is an operon required for uptake of nickel ions into the cell. It is present in many bacteria, but has been extensively studied in ''Helicobacter pylori''. Nickel is an essential nutrient for many microorganisms, where it participates in a variety of cellular processes. However, excessive levels of nickel ions in cell can be fatal to the cell. Nickel ion concentration in the cell is regulated through the ''nik'' operon.

Structure of the ''nik'' operon

The ''nik'' operon consists of six genes. The first five genes ''nikABCDE'' encode components of a typical ABC transport system and the last gene ''nikR'' encodes a DNA-binding protein that represses transcription of ''nikABCDE'' when sufficient Ni²⁺ is present. The ''nikR'' gene is located 5 bp downstream of the end of ''nikE'', transcribed in the same direction as ''nikABCDE''. The following table summarizes the structure of the ''nik'' operon:

Regulation

''nikR'' Regulation

Regulation of expression of the ''nikR'' gene is achieved by two promoters. The first is through the FNR regulon. The FNR controlled regulation of ''nikABCDE–nikR'' occurs at a FNR box located upstream of ''nikA'' at a putative NikR binding site. The second promoter element regulating ''nikR'' expression occurs 51 bp upstream of the ''nikR'' transcription start site and results in low-level constitutive expression. There is also evidence that ''nikR'' expression is partially autoregulated.

Regulation of Ni²⁺ uptake

Ni²⁺ is taken up into prokaryotic cells by one of two types of high-affinity transport systems. The first method involves ABC-type transporters (discussed in this article) and the second mechanism makes use of transition-metal permeases (such as HoxN of ''Ralstonia eutropha''). The ABC-type transporter system consists of five proteins, NikA–E, that carry out the ATP-dependent transport of Ni²⁺. NikA is a soluble, periplasmic, Ni-binding protein; NikB and NikC form a transmembrane pore for passage of Ni; and NikD and NikE hydrolyze ATP and couple this energy to Ni²⁺-transport. When Ni²⁺ is available in excess, NikR protein represses transcription of ''nikABCDE''.

Repression by NikR binding

Using profile-based sequence database searches, NikR was shown to be a member of the ribbon-helix-helix (RHH) family of transcription factors. It has been demonstrated that the N-terminal domain of NikR is responsible for binding to DNA and that it only binds in presence of Ni²⁺. NikR has two sites for binding to Ni²⁺ ions. Binding of Ni²⁺ at concentrations that allow full occupancy of only the high-affinity sites is sufficient for operator binding, but the affinity for the operator is increased 1000-fold and the operator footprints are larger when both nickel-binding sites are occupied. These results, combined with estimates of intracellular Ni²⁺ and NikR concentrations, lead to the conclusion that NikR is able to sense Ni²⁺ and regulate the ''nik'' operon expression over a range of intracellular Ni²⁺ concentrations from as low as one to as high as 10,000 molecules per cell.

See also

* gene regulation
* Operon
* lac operon

References

{{Reflist

Genetics
Nickel
Operons