ArticlePloS one2018
Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metal-associated domain.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 18 citations in OpenAlex.
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- Genome-wide identification of heavy-metal ATPases genes in Areca catechu: investigating their functionality under heavy metal exposure.BMC plant biology · 2024Article
- Hunting down zinc(II)-binding sites in proteins with distance matrices.Bioinformatics (Oxford, England) · 2023Article
- Article
- Uncharacterized Proteins CxORFx: Subinteractome Analysis and Prognostic Significance in Cancers.International journal of molecular sciences · 2023Article
- New Proteins Contributing to Immune Cell Infiltration and Pannus Formation of Synovial Membrane from Arthritis Diseases.International journal of molecular sciences · 2021Article
- Zincbindpredict-Prediction of Zinc Binding Sites in Proteins.Molecules (Basel, Switzerland) · 2021Article
- Proteomic Analyses ofFrontiers in cellular and infection microbiology · 2021Article
- Evolutionary compaction and adaptation visualized by the structure of the dormant microsporidian ribosome.Nature microbiology · 2019Article
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heavy metal-associated (HMA) domains bind metal ions at its Cys-x-x-Cys (CxxC) motif and constitute an intracellular network for trafficking of metal ions for utilization and detoxification. We thus expect that novel metalloproteins can be identified by screening proteins interacting with a HMA domain. In this study, we performed yeast two-hybrid screening of the human proteome and found an uncharacterized protein encoded as open reading frame 123 in chromosome 1 (C1orf123) that can interact specifically with the HMA domain of a copper chaperone for superoxide dismutase (CCSdI). Our X-ray structural analysis of C1orf123 further revealed that it binds a Zn2+ ion in a tetrahedral coordination with four thiolate groups from two conserved CxxC motifs. For the interaction between C1orf123 and CCSdI, the CxxC motifs in both C1orf123 and CCSdI were required, implying metal-mediated interaction through the CxxC motifs. Notably, C1orf123 did not interact with several other HMA domains containing CxxC motifs, supporting high specificity in the interaction between C1orf123 and CCSdI. Based upon these results, we further discuss functional and structural significance of the interaction between C1orf123 and CCS.
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