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

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Metallomics Vol - 7 Issue - 3

Metallomics Vol - 7 Issue - 2

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

Content Provider	Royal Society of Chemistry (RSC)
Author	Johnson, Ryan C. Merrell, D. Scott Maroney, Michael J. Hu, Heidi Q.
Copyright Year	2015
Abstract	Helicobacter pylori requires urease activity in order to survive in the acid environment of the human stomach. Urease is regulated in part by nickelation, a process that requires the HypA protein, which is a putative nickel metallochaperone that is generally associated with hydrogenase maturation. However, in H. pylori, HypA plays a dual role. In addition to an N-terminal nickel binding site, HypA proteins also contain a structural zinc site that is coordinated by two rigorously conserved CXXC sequences, which in H. pylori are flanked by His residues. These structural Zn sites are known to be dynamic, converting from Zn(Cys)4 centers at pH 7.2 to Zn(Cys)2(His)2 centers at pH 6.3 in the presence of Ni(II) ions. In this study, mutant strains of H. pylori that express zinc site variants of the HypA protein are used to show that the structural changes in the zinc site are important for the acid viability of the bacterium, and that a reduction in acid viability in these variants can be traced in large measure to deficient urease activity. This in turn leads to a model that connects the Zn(Cys)4 coordination to urease maturation.
Starting Page	674
Ending Page	682
Page Count	9
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	7
Issue Number	4
Journal	Metallomics
DOI	10.1039/c4mt00306c
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Hydrogenase N-terminus Helicobacter pylori PH Urease Nickel Mutation Protein Zinc CXXC
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

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

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