Abstract
The iron-containing protein neuroglobin (Ngb) involved in the transport of oxygen is generally considered the precursor of all animal globins. In this report, we studied the structure of Ngb of the cold-water sponge Halisarca dujardinii. In sponges, the oldest multicellular organisms, the Ngb gene contains three introns. In contrast to human Ngb, its promoter contains a TATA-box, rather than CG-rich motifs. In sponges, Ngb consists of 169 amino acids showing rather low similarity with its mammalian orthologues. It lacks Glu and Arg residues in positions required for prevention of hypoxia-related apoptosis. Nevertheless, Ngb contains both proximal and distal conserved heme-biding histidines. The primary structure of H. dujardinii neuroglobin predicted by sequencing was confirmed by mass-spectrometry analysis of recombinant Ngb expressed in E. coli. The high level of Ngb expression in sponge tissues suggests its possible involvement in the gas metabolism and presumably in other key metabolic processes in H. dujardinii.
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ACKNOWLEDGMENTS
The studies were carried out using the equipment of the Core Centrum of Institute of Developmental Biology RAS. Chromatography-mass spectrometric analysis was performed on the equipment of the Central Scientific-Practical Institute, Institute of Bioorganic Chemistry, Russian Academy of Sciences “New Materials and Technologies.”
Funding
The study was supported by the Russian Foundation for Basic Research (grant No. 19-34-50002). The work of KIA, OIK, ADF, VSM, NGG, and YVL was conducted under the IDB RAS Government basic research program in 2020.
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Adameyko, K.I., Kravchuk, O.I., Finoshin, A.D. et al. Structure of Neuroglobin from Cold-Water Sponge Halisarca dujardinii. Mol Biol 54, 416–420 (2020). https://doi.org/10.1134/S0026893320030036
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DOI: https://doi.org/10.1134/S0026893320030036