Nickel Homeostasis and Nickel Regulation: An Overview

2009 ◽  
Vol 109 (10) ◽  
pp. 4617-4643 ◽  
Author(s):  
Yanjie Li ◽  
Deborah B. Zamble
Keyword(s):  
2020 ◽  
Vol 228 (1) ◽  
pp. 163-178
Author(s):  
Haixiu Li ◽  
Yuan Liu ◽  
Huihui Qin ◽  
Xuelei Lin ◽  
Ding Tang ◽  
...  

2014 ◽  
Vol 43 (24) ◽  
pp. 8976-8989 ◽  
Author(s):  
Magdalena Rowinska-Zyrek ◽  
Jolanta Zakrzewska-Czerwinska ◽  
Anna Zawilak-Pawlik ◽  
Henryk Kozlowski

Nickel homeostasis inHelicobacter pyloriand potential histidine-rich binding sites from various bacterial and fungal pathogens are discussed.


2006 ◽  
Vol 74 (7) ◽  
pp. 3845-3852 ◽  
Author(s):  
Frank Nils Stähler ◽  
Stefan Odenbreit ◽  
Rainer Haas ◽  
Julia Wilrich ◽  
Arnoud H. M. Van Vliet ◽  
...  

ABSTRACT Maintaining metal homeostasis is crucial for the adaptation of Helicobacter pylori to the gastric environment. Iron, copper, and nickel homeostasis has recently been demonstrated to be required for the establishment of H. pylori infection in animal models. Here we demonstrate that the HP0969-0971 gene cluster encoding the Czc-type metal export pump homologs HP0969, HP0970, and the H. pylori-specific protein HP0971 forms part of a novel H. pylori metal resistance determinant, which is required for gastric colonization and for the modulation of urease activity. Insertional mutagenesis of the HP0971, HP0970, or HP0969 genes in H. pylori reference strain 26695 resulted in increased sensitivity to cadmium, zinc, and nickel (czn), suggesting that the encoded proteins constitute a metal-specific export pump. Accordingly, the genes were designated cznC (HP0971), cznB (HP0970), and cznA (HP0969). The CznC and CznA proteins play a predominant role in nickel homeostasis, since only the cznC and cznA mutants but not the cznB mutant displayed an 8- to 10-fold increase in urease activity. Nickel-specific affinity chromatography demonstrated that recombinant versions of CznC and CznB can bind to nickel and that the purified CznB protein interacted with cadmium and zinc, since both metals competitively inhibited nickel binding. Finally, single cznA, cznB, and cznC mutants did not colonize the stomach in a Mongolian gerbil-based animal model. This demonstrates that the metal export functions of H. pylori cznABC are essential for gastric colonization and underlines the extraordinary importance of metal ion homeostasis for the survival of H. pylori in the gastric environment.


2008 ◽  
Vol 2008 ◽  
pp. 1-6 ◽  
Author(s):  
Xuesong Sun ◽  
Ruiguang Ge ◽  
Jen-Fu Chiu ◽  
Hongzhe Sun ◽  
Qing-Yu He

Helicobacter pylori (H. pylori) is a widespread human pathogen causing peptic ulcers and chronic gastritis. Maintaining nickel homeostasis is crucial for the establishment of H. pylori infection in humans. We used immobilized-nickel affinity chromatography to isolate Ni-related proteins from H. pylori cell extracts. Two-dimensional gel electrophoresis and mass spectrometry were employed to separate and identify twenty two Ni-interacting proteins in H. pylori. These Ni-interacting proteins can be classified into several general functional categories, including cellular processes (HspA, HspB, TsaA, and NapA), enzymes (Urease, Fumarase, GuaB, Cad, PPase, and DmpI), membrane-associated proteins (OM jhp1427 and HpaA), iron storage protein (Pfr), and hypothetical proteins (HP0271, HP jhp0216, HP jhp0301, HP0721, HP0614, and HP jhp0118). The implication of these proteins in nickel homeostasis is discussed.


Author(s):  
James A. Budnick ◽  
Clayton C. Caswell
Keyword(s):  

2006 ◽  
Vol 62 (1) ◽  
pp. 252-262 ◽  
Author(s):  
Jeffrey S. Iwig ◽  
Jessica L. Rowe ◽  
Peter T. Chivers

ChemInform ◽  
2010 ◽  
Vol 41 (9) ◽  
Author(s):  
Yanjie Li ◽  
Deborah B. Zamble
Keyword(s):  

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