A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life

Haas, Crysten E.; Rodionov, Dmitry A.; Kropat, Janette; Malasarn, Davin; Merchant, Sabeeha; Crécy‐Lagard, Valérie de

doi:10.1186/1471-2164-10-470

Cited by 142 publications

(224 citation statements)

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“…A recent exhaustive bioinformatic analysis classified members of the COG0523 family into 15 subfamilies (24). That study proposed that several of these subfamilies have a role in survival under conditions of deficient zinc nutrition and are frequently associated with Zur-binding sites in diverse bacteria (24). Consistent with this, Bacillus subtilis mutants defective in a protein of the COG0523 family exhibit a growth defect in low-zinc medium (19).…”

Section: Discussionmentioning

confidence: 96%

“…However, All4722 contains 19 His residues, whereas All1751 contains only 2. all1197 is also in this category although its product has a deletion in the N-terminal domain and a single histidine in the C-terminal domain. A recent exhaustive bioinformatic analysis classified members of the COG0523 family into 15 subfamilies (24). That study proposed that several of these subfamilies have a role in survival under conditions of deficient zinc nutrition and are frequently associated with Zur-binding sites in diverse bacteria (24).…”

Section: Discussionmentioning

confidence: 99%

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Characterization of the Response to Zinc Deficiency in the Cyanobacterium Anabaena sp. Strain PCC 7120

Napolitano

Rubio

Santamaría-Gómez

et al. 2012

Journal of Bacteriology

101

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bZur regulators control zinc homeostasis by repressing target genes under zinc-sufficient conditions in a wide variety of bacteria. This paper describes how part of a survey of duplicated genes led to the identification of the open reading frame all2473 as the gene encoding the Zur regulator of the cyanobacterium Anabaena sp. strain PCC 7120. All2473 binds to DNA in a zinc-dependent manner, and its DNA-binding sequence was characterized, which allowed us to determine the relative contribution of particular nucleotides to Zur binding. A zur mutant was found to be impaired in the regulation of zinc homeostasis, showing sensitivity to elevated concentrations of zinc but not other metals. In an effort to characterize the Zur regulon in Anabaena, 23 genes containing upstream putative Zur-binding sequences were identified and found to be regulated by Zur. These genes are organized in six single transcriptional units and six operons, some of them containing multiple Zur-regulated promoters. The identities of genes of the Zur regulon indicate that Anabaena adapts to conditions of zinc deficiency by replacing zinc metalloproteins with paralogues that fulfill the same function but presumably with a lower zinc demand, and with inducing putative metallochaperones and membrane transport systems likely being involved in the scavenging of extracellular zinc, including plasma membrane ABC transport systems and outer membrane TonB-dependent receptors. Among the Zur-regulated genes, the ones showing the highest induction level encode proteins of the outer membrane, suggesting a primary role for components of this cell compartment in the capture of zinc cations from the extracellular medium.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Characterization of the Response to Zinc Deficiency in the Cyanobacterium Anabaena sp. Strain PCC 7120

Napolitano

Rubio

Santamaría-Gómez

et al. 2012

Journal of Bacteriology

101

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“…15 Specifically, there is significant similarity between the ReNHase TG328-2 activator protein and the COG0523 subgroup of the G3E family of P-loop GTPases. COG0523 constitutes a diverse group of proteins with unknown function and wide distribution, while permission has been granted for this version to appear in e-Publications@Marquette.…”

Section: Sequence Analysismentioning

confidence: 99%

The iron-type nitrile hydratase activator protein is a GTPase

Gumataotao

Lankathilaka

Bennett

et al. 2017

Biochemical Journal

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Abstract:The Fe-type nitrile hydratase activator protein from Rhodococcus equi TG328-2 (ReNHase TG328-2) was successfully expressed and purified. Sequence analysis and homology modeling suggest that it is a G3E P-loop guanosine triphosphatase (GTPase) within the COG0523 subfamily. Kinetic studies revealed that the Fe-type activator protein is capable of hydrolyzing NOT THE PUBLISHED VERSION; this is the author's final, peer-reviewed manuscript. The published version may be accessed by following the link in the citation at the bottom of the page.Biochemical Journal, Vol 474, No. 2 (January 15, 2017): pg. 247-258. DOI. This article is © Portland Press Limited and permission has been granted for this version to appear in e-Publications@Marquette. Portland Press Limited does not grant permission for this article to be further copied/distributed or hosted elsewhere without the express permission from Portland Press Limited. 2GTP to GDP with a kcat value of 1.2 × 10 −3 s −1 and a Km value of 40 μM in the presence of 5 mM MgCl2 in 50 mM 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid at a pH of 8.0. The addition of divalent metal ions, such as Co(II), which binds to the ReNHase TG328-2 activator protein with a Kd of 2.9 μM, accelerated the rate of GTP hydrolysis, suggesting that GTP hydrolysis is potentially connected to the proposed metal chaperone function of the ReNHase TG328-2 activator protein. Circular dichroism data reveal a significant conformational change upon the addition of GTP, which may be linked to the interconnectivity of the cofactor binding sites, resulting in an activator protein that can be recognized and can bind to the NHase α-subunit. A combination of these data establishes, for the first time, that the ReNHase TG328-2 activator protein falls into the COG0523 subfamily of G3E P-loop GTPases, many of which play a role in metal homeostasis processes.

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“…Zincsparing mechanisms and zinc protein assembly are presently underinvestigated in plants and ripe for exploitation. Proteins carrying a COG0523 domain, which is suggested to function in zinc homeostasis in all kingdoms of life (Haas et al, 2009), might be involved in plant zinc homeostasis.…”

Section: Economy Supply and Demandmentioning

confidence: 99%

The Elements of Plant Micronutrients

Merchant

2010

Plant Physiology

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Amino acid R groups in proteins provide a limited repertoire of functional groups for catalyzing biochemical transformations. The use of inorganic elements, particularly the first row transition metals, expands greatly the range of chemistry that can be catalyzed in a cell. Zinc ions are key for enzymatic catalysis of reactions that require an electrophile, while iron, manganese, copper, nickel, and molybdenum are brokers of redox transformations. These elements are therefore essential nutrients for plants. They are referred to as micronutrients because they are less abundant (by 1-4 orders of magnitude) compared to the macronutrients like sulfur and phosphorus. Even among the micronutrients, the amount of individual transition metals in plant tissues varies over several orders of magnitude, with iron being the most abundant (approximately 100 mg/g) and molybdenum the least (Fig. 1).Each metal has unique chemical properties including ligand preferences, coordination geometries, and redox potentials, which are exploited for diverse, yet highly specific, chemistry. In the photosynthetic electron transfer chain, the midpoint potentials of the metal centers span nearly 1.5 V. The import of metals in biology is evident from the association of approximately 30% to 40% of proteins with a metal . Transition metal-protein associations are highly specific, at least in vivo, because mismetallation can block activity or yield undesirable chemistry. In vitro, the associations occur according to thermodynamic preferences described by the Irving-Williams series: For divalent ions, copper and zinc ions bind most tightly relative to manganese and iron ions .The in vivo specificity is achieved by kinetic control of metal ion assimilation, distribution, and storage and of metalloprotein assembly, or in other words, metal metabolism. For nickel and copper proteins in bacteria, specificity can be achieved by direct protein to protein transfer via metallochaperones coupled with structural reorganization and stabilization of the resulting holoprotein so that the metal is kinetically trapped. For a periplasmic manganese protein in bacteria, one study showed that correct metallation is achieved by restricting holoprotein formation to the cytoplasm where the concentration of another competing metal ion is reduced by sequestration in binding protein (Tottey et al., 2008). Compartmentation of metal ions is, therefore, a key consideration in metalloprotein biogenesis pathways.Nonessential metals like cadmium, mercury, and silver can compete with the essential transition metals for uptake and metalloprotein assembly pathways because protein flexibility can reduce the selectivity of metal-binding sites. A consequence of the redox reactivity and the promiscuous binding of transition metals to thiol, thioether, imidazole, and carboxylate ligands is that inappropriate accumulation of metals is harmful in biology. Therefore, metal metabolism is under homeostatic regulation (plant homeostasis pathways reviewed in Palmer and Guerinot, 2009).Studies...

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A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life

Cited by 142 publications

References 123 publications

Characterization of the Response to Zinc Deficiency in the Cyanobacterium Anabaena sp. Strain PCC 7120

Characterization of the Response to Zinc Deficiency in the Cyanobacterium Anabaena sp. Strain PCC 7120

The iron-type nitrile hydratase activator protein is a GTPase

The Elements of Plant Micronutrients

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