Transphyletic conservation of nitric oxide synthase regulation in cephalochordates and tunicates
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ORIGINAL ARTICLE
Transphyletic conservation of nitric oxide synthase regulation in cephalochordates and tunicates Filomena Caccavale 1 & Ugo Coppola 1,2 & Quirino A. Vassalli 1,3 & Claudia La Vecchia 1 & Anna Palumbo 1 & Enrico D’Aniello 1 & Annamaria Locascio 1 & Filomena Ristoratore 1 & Salvatore D’Aniello 1 Received: 29 November 2019 / Accepted: 16 August 2020 # Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Nitric oxide synthase is ubiquitously present in metazoans and is involved in a wide range of biological processes. Three distinct Nos genes have been so far identified in vertebrates exhibiting a complex expression pattern and transcriptional regulation. Nevertheless, although independent events of Nos duplication have been observed in several taxa, only few studies described the regulatory mechanisms responsible for their activation in non-vertebrate animals. To shed light on the mechanisms underlying neuronal-type Nos expression, we focused on two non-vertebrate chordates: the cephalochordate Branchiostoma lanceolatum and the tunicate Ciona robusta. Here, throughout transphyletic and transgenic approaches, we identified genomic regions in both species acting as Nos functional enhancers during development. In vivo analyses of Nos genomic fragments revealed their ability to recapitulate the endogenous expression territories. Therefore, our results suggest the existence of evolutionary conserved mechanisms responsible for neuronal-type Nos regulation in non-vertebrate chordates. In conclusion, this study paves the way for future characterization of conserved transcriptional logic underlying the expression of neuronal-type Nos genes in chordates. Keywords Neuronal-type NOS . Gene regulation . Transgenesis . Evolution . Development . Chordates
Introduction Nitric oxide synthase (Nos) is the enzyme responsible for the production of nitric oxide (NO) in the cell. In vertebrates three distinct Nos, carrying structural and functional specializations, have been identified: the constitutive Nos1 (neuronal-type Nos) and Nos3 (endothelial-type Nos) and the inducible Nos2 (Alderton et al. 2001). These enzymes are characterized Communicated by Hiroki Nishida Electronic supplementary material The online version of this article (https://doi.org/10.1007/s00427-020-00668-3) contains supplementary material, which is available to authorized users. * Salvatore D’Aniello [email protected] 1
Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn Napoli, Villa Comunale, 80121 Napoli, Italy
2
Present address: The Heart Institute and Division of Molecular Cardiovascular Biology, Cincinnati Children’s Hospital Medical Center, Cincinnati, OH, USA
3
Present address: Scripps Research, 10466 N Torrey Pines Rd, La Jolla, CA 92037, USA
by a reductase and an oxygenase domain, containing specific binding sites for cofactors like heme, tetrahydrobiopterin (BH4), calmodulin (CaM), flavin mononucleotide (FMN), flavin adenine dinucleotide (FAD), and nicotinamide adenine dinucleotide phosp
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