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Cited by 44Metalloenzymes and iron-sulfur proteinsBacterial Genetics and BiotechnologyTrace Elements in Health

COG0523 proteins: a functionally diverse family of transition metal-regulated G3E P-loop GTP hydrolases from bacteria to man

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Edmonds, Katherine A, Jordan, Matthew R, Giedroc, David P·2021·Metallomics
DOI 10.1093/mtomcs/mfab046PMC PMC8360895
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Abstract

Transition metal homeostasis ensures that cells and organisms obtain sufficient metal to meet cellular demand while dispensing with any excess so as to avoid toxicity. In bacteria, zinc restriction induces the expression of one or more Zur (zinc-uptake repressor)-regulated Cluster of Orthologous Groups (COG) COG0523 proteins. COG0523 proteins encompass a poorly understood sub-family of G3E P-loop small GTPases, others of which are known to function as metallochaperones in the maturation of cobalamin (CoII) and NiII cofactor-containing metalloenzymes. Here, we use genomic enzymology tools to functionally analyse over 80 000 sequences that are evolutionarily related to Acinetobacter baumannii ZigA (Zur-inducible GTPase), a COG0523 protein and candidate zinc metallochaperone. These sequences segregate into distinct sequence similarity network (SSN) clusters, exemplified by the ZnII-Zur-regulated and FeIII-nitrile hydratase activator CxCC (C, Cys; X, any amino acid)-containing COG0523 proteins (SSN cluster 1), NiII-UreG (clusters 2, 8), CoII-CobW (cluster 4), and NiII-HypB (cluster 5). A total of five large clusters that comprise ≈ 25% of all sequences, including cluster 3 which harbors the only structurally characterized COG0523 protein, Escherichia coli YjiA, and many uncharacterized eukaryotic COG0523 proteins. We also establish that mycobacterial-specific protein Y (Mpy) recruitment factor (Mrf), which promotes ribosome hibernation in actinomycetes under conditions of ZnII starvation, segregates into a fifth SSN cluster (cluster 17). Mrf is a COG0523 paralog that lacks all GTP-binding determinants as well as the ZnII-coordinating Cys found in CxCC-containing COG0523 proteins. On the basis of this analysis, we discuss new perspectives on the COG0523 proteins as cellular reporters of widespread nutrient stress induced by ZnII limitation.

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  • Thiol-dependent ligand exchange reactions underlie the ability of COG0523 family proteins to function as GTP-activated Zn2+ metallochaperones to direct the flow of Zn2+ to the most important client proteins under conditions of Zn limitation.

    “Thiol-dependent ligand exchange reactions also underlie the ability of COG0523 family proteins to function as GTP-activated Zn2+ metallochaperones to direct the flow of Zn2+ to the most important client proteins under conditions of Zn limitation.213−217”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [215]

    The section on metalloproteome status under transition-metal restriction describes COG0523-mediated Zn²⁺ prioritization to specific client enzymes during Zn limitation. The structural-insights section proposes that metal-binding cysteines facilitate ligand exchange after GTP hydrolysis, but explicitly calls this model untested. The claim overstates that proposed thiol-dependent mechanism as established for the family. (LLM, conf=0.88)

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Cited by

Sorted by citations

Authors
Edmonds, K. A., Jordan, M. R., & Giedroc, D. P.
Affiliations
Indiana University Bloomington (US)
Corresponding author
Giedroc, David P
ORCID
Venue
Metallomics
Publisher
Oxford University Press (OUP)
Published
2021-07-24
Volume
13
Issue
8
ISSN
  • 1756-5901 (ISSN-L)
  • 1756-591X
DOI
10.1093/mtomcs/mfab046
PMC
PMC8360895
OpenAlex
W3184756130
Cited by
44
References
8
Citations by year
2026: 11 · 2025: 13 · 2024: 4 · 2023: 5 · 2022: 9 · 2021: 2
FWCI
0.92
Type
journal article
Language
en
Open access
Licence
academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
Locations
  • Metallomics (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (R35 GM118157, R01 AI110171)
  • Indiana University Graduate Training Program in Quantitative and Chemical Biology (GM109825, GM131994)
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords
transition metal homeostasis, metallochaperone, ribosome hibernation, sequence similarity networks, nutritional stress, Acinetobacter baumannii, Escherichia coli
MeSH terms
Animals, Bacteria, Bacterial Proteins, Biological Evolution, Humans, Hydrolases, Metals, GTP Phosphohydrolases, Genomics, Transition Elements, Mice, Metallochaperones

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