NDLI: Nickel translocation between metallochaperones HypA and UreE in Helicobacter pylori

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Metallomics Vol - 6 Issue - 8

Metallomics Vol - 6 Issue - 7

Metallomics Vol - 6 Issue - 6

Metallomics Vol - 6 Issue - 5

Metallomics Vol - 6 Issue - 4

Metallomics Vol - 6 Issue - 3

Metallomics Vol - 6 Issue - 2

Nickel translocation between metallochaperones HypA and UreE in Helicobacter pylori

Content Provider	Royal Society of Chemistry (RSC)
Author	Xia, Wei Li, Hongyan Yang, Xinming Lai, Yau-Tsz Sun, Hongzhe Cheng, Tianfan
Copyright Year	2014
Abstract	Incorporation of nickel ions to the active sites of urease and hydrogenase is prerequisite for the appropriate functions of the metalloenzymes. Such a process requires the participation of several accessory proteins. Interestingly, some of them are shared by the two enzymes in their maturation processes. In this work, we characterized the molecular details of the interaction of metallochaperones UreE and HypA in Helicobacter pylori. We show by chemical cross-linking and static light scattering that the UreE dimer binds to HypA to form a hetero-complex i.e. HypA–(UreE)2. The dissociation constant (Kd) of the protein complex was determined by ITC to be 1 μM in the absence of nickel ions; whereas binding of Ni2+ but not Zn2+ to UreE resulted in ca. one fold decrease in the affinity. The putative interfaces on HypA unveiled by NMR chemical shift perturbation were found mainly at the nickel binding domain and in the cleft between α1 and β1/β6. We also identified that the C-domain of UreE, in particular the C-terminal residues of 158–170 are indispensable for the interaction of UreE and HypA. Such an interaction was also observed intracellularly by GFP-fragment reassembly assay. Moreover, we demonstrated using a fluorescent probe that nickel is transferred from HypA to UreE via the specific protein–protein interaction. Deletion of the C-terminus (residues 158–170) of UreE abolished nickel transfer and led to a significant decrease in urease activity. This study provides direct in vitro and in vivo evidence as well as molecular details of nickel translocation mediated by protein–protein interaction.
Starting Page	1731
Ending Page	1736
Page Count	6
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	6
Issue Number	9
Journal	Metallomics
DOI	10.1039/c4mt00134f
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Protein\u2013protein interaction Static light scattering Dissociation constant Urease Cross-link Protein dimer Protein C-terminus Hydrogenase Chemical shift Helicobacter pylori ITC Nickel Isothermal titration calorimetry Nuclear magnetic resonance
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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Dynamic HypA zinc site is essential for acid viability and proper urease maturation in Helicobacter pylori

Interaction between the Helicobacter pylori accessory proteins HypA and UreE is needed for urease maturation (2007)

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UreE-UreG Complex Facilitates Nickel Transfer and Preactivates GTPase of UreG in Helicobacter pylori

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Nickel translocation between metallochaperones HypA and UreE in Helicobacter pylori