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Vol 57(2023) N 6 p. 1085-1096; DOI 10.1134/S0026893323060109  O.I. Kravchuk1*, A.D. Finoshin1, K.V. Mikhailov2,3, R.H. Ziganshin4, K.I. Adameyko1, N.G. Gornostaev1, A.I. Zhurakovskaya1, V.S. Mikhailov1, E.I. Shagimardanova5, Yu.V. Lyupina1 Characteristics of δ-Aminolevulinic Acid Dehydratase of the Cold-Water Sponge Halisarca dujardinii 1Koltsov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334 Russia2Belozersky Institute of Physicochemical Biology, Moscow State University, Moscow, 119992 Russia 3Kharkevich Institute for Information Transmission Problems, Russian Academy of Sciences, Moscow, 127051 Russia 4Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997 Russia 5Regulatory Genomics Research Center, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, 420012 Russia *kravchuk444@mail.ru Received - 2023-04-11; Revised - 2023-06-02; Accepted - 2023-06-20 δ-Aminolevulinic acid dehydratase (ALAD) is a key enzyme of the cytoplasmic heme biosynthesis pathway. The primary structure of the ALAD gene, the multimeric structure of the ALAD/hemB protein, and ALAD expression during the annual reproductive cycle were studied in the cold-water marine sponge Halisarca dujardinii. The results implicated the GATA-1 transcription factor and DNA methylation in regulating ALAD expression. Re-aggregation of sponge cells was accompanied by a decrease in ALAD expression and a change in the cell content of an active ALAD/hemB form. Further study of heme biosynthesis and the role of ALAD/hemB in morphogenesis of basal animals may provide new opportunities for treating pathologies in higher animals. heme biosynthesis, δ-aminolevulinic acid dehydratase, basal animals, plasticity |
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