ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2011
Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Design of a Novel Diamine Biosensor to Guide the Engineering of Escherichia coli for Cadaverine Overproduction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- 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
- Structural investigations connect the disordered N-terminal extension of HypB to the activities of HypB and SlyD in E. coli.Protein science : a publication of the Protein Society · 2025Article
- Article
- Mechanistic Insights into the Metal-Dependent Activation of ZnInorganic chemistry · 2019Article
- Bimodal Nickel-Binding Site onInorganic chemistry · 2019Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- The relationship between folding and activity in UreG, an intrinsically disordered enzyme.Scientific reports · 2017Article
- High-affinity metal binding by the Escherichia coli [NiFe]-hydrogenase accessory protein HypB is selectively modulated by SlyD.Metallomics : integrated biometal science · 2017Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- Structure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori urease.PLoS biology · 2013Article
- Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.Biochemistry · 2013Article
- Metal binding properties of Escherichia coli YjiA, a member of the metal homeostasis-associated COG0523 family of GTPases.Biochemistry · 2013Article
- YeiR: a metal-binding GTPase from Escherichia coli involved in metal homeostasis.Metallomics : integrated biometal science · 2012Article
- Structural basis for GTP-dependent dimerization of hydrogenase maturation factor HypB.PloS one · 2012Article
- Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation.PloS one · 2012Article
- Escherichia coli SlyD, more than a Ni(II) reservoir.Biochemistry · 2011Article
- Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Biosynthesis of the metallocenter in the active site of the [NiFe] hydrogenase enzyme requires the accessory protein HypB, which is a metal-binding GTPase. In this study, the interplay between the individual activities of Escherichia coli HypB was examined. The full-length protein undergoes nucleotide-responsive dimerization that is disrupted upon mutation of L242 and L246 to alanine. This mutant HypB is monomeric under all of the conditions investigated but the inability of L242A/L246A HypB to dimerize does not abolish its GTPase activity and the monomeric protein has metal-binding behavior similar to that of wild-type HypB. Furthermore, expression of L242A/L246A HypB in vivo results in hydrogenase activity that is approximately half of the activity produced by the wild-type control, suggesting that dimerization of HypB does not have a critical role in the hydrogenase maturation pathway. In contrast, the GTPase activity of HypB is modulated by metal loading of the protein. These results provide insight into the role of HypB in hydrogenase biosynthesis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.