Conservative and Atypical Ferritins of Sponges.

Autor:	Adameyko KI; N.K. Koltzov Institute of Developmental Biology, Russian Academy of Sciences, 119334 Moscow, Russia., Burakov AV; A.N. Belozersky Institute of Physical and Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia., Finoshin AD; N.K. Koltzov Institute of Developmental Biology, Russian Academy of Sciences, 119334 Moscow, Russia., Mikhailov KV; A.N. Belozersky Institute of Physical and Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.; A.A. Kharkevich Institute for Information Transmission Problems, Russian Academy of Sciences, 127051 Moscow, Russia., Kravchuk OI; N.K. Koltzov Institute of Developmental Biology, Russian Academy of Sciences, 119334 Moscow, Russia., Kozlova OS; Extreme Biology Laboratory, Institute of Fundamental Medicine and Biology, Kazan Federal University, 420111 Kazan, Russia., Gornostaev NG; N.K. Koltzov Institute of Developmental Biology, Russian Academy of Sciences, 119334 Moscow, Russia., Cherkasov AV; Center of Life Sciences, Skolkovo Institute of Science and Technology, 143026 Moscow, Russia., Erokhov PA; N.K. Koltzov Institute of Developmental Biology, Russian Academy of Sciences, 119334 Moscow, Russia., Indeykina MI; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia., Bugrova AE; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia., Kononikhin AS; Center for Computational and Data-Intensive Science and Engineering, Skolkovo Institute of Science and Technology, 143026 Moscow, Russia., Moiseenko AV; Faculty of Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia., Sokolova OS; Faculty of Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia., Bonchuk AN; Institute of Gene Biology, Russian Academy of Sciences, 119334 Moscow, Russia., Zhegalova IV; A.A. Kharkevich Institute for Information Transmission Problems, Russian Academy of Sciences, 127051 Moscow, Russia.; Center of Life Sciences, Skolkovo Institute of Science and Technology, 143026 Moscow, Russia.; Faculty of Bioengineering and Bioinformatics, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia., Georgiev AA; Faculty of Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia., Mikhailov VS; N.K. Koltzov Institute of Developmental Biology, Russian Academy of Sciences, 119334 Moscow, Russia., Gogoleva NE; Extreme Biology Laboratory, Institute of Fundamental Medicine and Biology, Kazan Federal University, 420111 Kazan, Russia., Gazizova GR; Extreme Biology Laboratory, Institute of Fundamental Medicine and Biology, Kazan Federal University, 420111 Kazan, Russia., Shagimardanova EI; Extreme Biology Laboratory, Institute of Fundamental Medicine and Biology, Kazan Federal University, 420111 Kazan, Russia., Gusev OA; Extreme Biology Laboratory, Institute of Fundamental Medicine and Biology, Kazan Federal University, 420111 Kazan, Russia.; Department of Regulatory Transcriptomics for Medical Genetic Diagnostics, Graduate School of Medical Sciences, Juntendo University, Tokyo 113-8421, Japan.; RIKEN Center for Integrative Medical Sciences, RIKEN, Yokohama 351-0198, Japan., Lyupina YV; N.K. Koltzov Institute of Developmental Biology, Russian Academy of Sciences, 119334 Moscow, Russia.
Jazyk:	angličtina
Zdroj:	International journal of molecular sciences [Int J Mol Sci] 2021 Aug 11; Vol. 22 (16). Date of Electronic Publication: 2021 Aug 11.
DOI:	10.3390/ijms22168635
Abstrakt:	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.
Databáze:	MEDLINE
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