4.7 Article

Conservative and Atypical Ferritins of Sponges

Journal

Publisher

MDPI
DOI: 10.3390/ijms22168635

Keywords

ferritin; heme; globins; iron; sponges; Halisarca dujardini; Halichondria panicea; invertebrates; whole body regeneration

Funding

  1. Ministry of Science and Higher Education of the Russian Federation [075-15-2020-773]

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Ferritins are a conservative family of proteins found in all species, playing essential roles in resistance to redox stress, immune response, and cell differentiation. The study characterized ferritins in two cold-water sponges, revealing their regulation by cellular iron and oxygen levels, and their importance in various biological processes. Further research is needed to explore the function of atypical ferritins lacking iron-binding capacity in invertebrate species.
Ferritins comprise a conservative family of proteins found in all species and play an essential role in resistance to redox stress, immune response, and cell differentiation. Sponges (Porifera) are the oldest Metazoa that show unique plasticity and regenerative potential. Here, we characterize the ferritins of two cold-water sponges using proteomics, spectral microscopy, and bioinformatic analysis. The recently duplicated conservative HdF1a/b and atypical HdF2 genes were found in the Halisarca dujardini genome. Multiple related transcripts of HpF1 were identified in the Halichondria panicea transcriptome. Expression of HdF1a/b was much higher than that of HdF2 in all annual seasons and regulated differently during the sponge dissociation/reaggregation. The presence of the MRE and HRE motifs in the HdF1 and HdF2 promotor regions and the IRE motif in mRNAs of HdF1 and HpF indicates that sponge ferritins expression depends on the cellular iron and oxygen levels. The gel electrophoresis combined with specific staining and mass spectrometry confirmed the presence of ferric ions and ferritins in multi-subunit complexes. The 3D modeling predicts the iron-binding capacity of HdF1 and HpF1 at the ferroxidase center and the absence of iron-binding in atypical HdF2. Interestingly, atypical ferritins lacking iron-binding capacity were found in genomes of many invertebrate species. Their function deserves further research.

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