Transcriptional Contribution of Transposable Elements in Relation to Salinity Conditions in Teleosts and Silencing Mechanisms Involved

Autor:	Elisa Carotti, Federica Carducci, Samuele Greco, Marco Gerdol, Daniele Di Marino, Nunzio Perta, Anna La Teana, Adriana Canapa, Marco Barucca, Maria Assunta Biscotti
Přispěvatelé:	Carotti, Elisa, Carducci, Federica, Greco, Samuele, Gerdol, Marco, Di Marino, Daniele, Perta, Nunzio, La Teana, Anna, Canapa, Adriana, Barucca, Marco, Biscotti, Maria Assunta
Rok vydání:	2022
Předmět:	Gills fish silencing mechanisms silencing mechanism animal structures Organic Chemistry Oryzias Fresh Water General Medicine transposable element Catalysis salinity Computer Science Applications Inorganic Chemistry Oncorhynchus keta transposable elements Krüppel-associated box domain zinc finger proteins (KRAB-ZFPs) DNA Transposable Elements Animals Physical and Theoretical Chemistry Molecular Biology Spectroscopy
Zdroj:	International Journal of Molecular Sciences; Volume 23; Issue 9; Pages: 5215
ISSN:	1422-0067
Popis:	Fish are an interesting taxon comprising species adapted to a wide range of environments. In this work, we analyzed the transcriptional contribution of transposable elements (TEs) in the gill transcriptomes of three fish species exposed to different salinity conditions. We considered the giant marbled eel Anguilla marmorata and the chum salmon Oncorhynchus keta, both diadromous, and the marine medaka Oryzias melastigma, an euryhaline organism sensu stricto. Our analyses revealed an interesting activity of TEs in the case of juvenile eels, commonly adapted to salty water, when exposed to brackish and freshwater conditions. Moreover, the expression assessment of genes involved in TE silencing mechanisms (six in heterochromatin formation, fourteen known to be part of the nucleosome remodeling deacetylase (NuRD) complex, and four of the Argonaute subfamily) unveiled that they are active. Finally, our results evidenced for the first time a krüppel-associated box (KRAB)-like domain specific to actinopterygians that, together with TRIM33, might allow the functioning of NuRD complex also in fish species. The possible interaction between these two proteins was supported by structural prediction analyses.
Databáze:	OpenAIRE
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