<i>Danionella dracula</i>

Abstract


The purpose of this project is to identify and describe the selenoproteins present in the genome of Danionella dracula, a sweetwater fish identified in 2009 in Myanmar. Selenoproteins are proteins that contain selenocysteine (U, Sec), a non-standard amino acid which contains selenium. Selenoproteins are mainly involved in redox metabolism, but a few of them have a structural function. Selenocysteine is coded by an UGA codon, which normally serves as a stop codon, so in order to be translated these selenoproteins need extra proteic machinery that modifies the normal translation process.
[1,2]

In order to accomplish the identification of Danionella dracula’s selenoproteome, we have compared its genome to that of Danio rerio, a well-known and annotated fish species that is commonly used as a reference organism and is closely related to Danionella dracula. Our findings through this comparison and analysis consist of 40 proteins, 8 of which are cysteine homologues of selenoproteins, and 4 of which are part of the selenoprotein machinery. We have found some deletions and less duplications than we would have expected, and these findings might fit with the developmentally stunted nature of Danionella dracula.
[1,3,11]