ArticleJournal of bacteriology2005
Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 78 citations in OpenAlex.
- The HypA and HypB metallochaperones from Methanococcus maripaludis have unique metal-binding properties and a distinct nickel transfer mechanism.The Journal of biological chemistry · 2026Article
- Bimodal Nickel-Binding Site onInorganic chemistry · 2019Article
- The Metallochaperone Encoding GeneMicroorganisms · 2019Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- Crystal structures of a [NiFe] hydrogenase large subunit HyhL in an immature state in complex with a Ni chaperone HypA.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Glutamate Ligation in the Ni(II)- and Co(II)-Responsive Escherichia coli Transcriptional Regulator, RcnR.Inorganic chemistry · 2017Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A moonlighting function of Mycobacterium smegmatis Ku in zinc homeostasis?Protein science : a publication of the Protein Society · 2015Article
- Relationship between Ni(II) and Zn(II) coordination and nucleotide binding by the Helicobacter pylori [NiFe]-hydrogenase and urease maturation factor HypB.The Journal of biological chemistry · 2014Article
- Nickel trafficking system responsible for urease maturation in Helicobacter pylori.World journal of gastroenterology · 2013Review
- Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.Biochemistry · 2013Article
- Effects of select histidine to cysteine mutations on transcriptional regulation by Escherichia coli RcnR.Biochemistry · 2013Article
- Specific metal recognition in nickel trafficking.Biochemistry · 2012Review
- Helicobacter pylori hydrogenase accessory protein HypA and urease accessory protein UreG compete with each other for UreE recognition.Biochimica et biophysica acta · 2012Article
- ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-X-X-Cys Redox Centres and Iron-Based Oxidative Stress.Journal of signal transduction · 2012Article
- Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation.PloS one · 2012Article
- Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase.The Journal of biological chemistry · 2011Article
- Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.The Journal of biological chemistry · 2011Article
- Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hyp operon encodes accessory proteins that are required for the maturation of the [NiFe] hydrogenase enzymes and, in some organisms, for the production of urease enzymes as well. HypA or a homologous protein is required for nickel insertion into the hydrogenase precursor proteins. In this study, recombinant HypA from Escherichia coli was purified and characterized in vitro. Metal analysis was used to demonstrate that HypA simultaneously binds stoichiometric Zn(2+) and stoichiometric Ni(2+). Competition experiments with a metallochromic indicator reveal that HypA binds zinc with nanomolar affinity. Spectroscopic analysis of cobalt-containing HypA provides evidence for a tetrathiolate coordination sphere, suggesting that the zinc site has a structural role. In addition, HypA can exist as several oligomeric complexes and the zinc content modulates the quaternary structure of the protein. Fluorescence titration experiments demonstrate that HypA binds nickel with micromolar affinity and that the presence of zinc does not dramatically affect the nickel-binding activity. Finally, complex formation between HypA and HypB, another accessory protein required for nickel insertion, was observed. These experiments suggest that HypA is an architectural component of the hydrogenase metallocenter assembly pathway and that it may also have a direct role in the delivery of nickel to the hydrogenase large subunit.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.