Structural and functional studies of STAT1 from Atlantic salmon (Salmo salar).

BACKGROUND:Type I and type II interferons (IFNs) exert their effects mainly through the pathway, which is presently best described in mammals. is involved in signaling pathways induced by both types of IFNs. It has a domain-like structure including an amino-terminus that stabilizes interaction between dimers in a promoter-binding situation, a coiled coil domain facilitating interactions to other proteins, a central DNA-binding domain, a SH2 domain responsible for dimerization of phosphorylated and conserved phosphorylation sites within the carboxy terminus. The latter is also the transcriptional activation domain. RESULTS:A salmon (Salmo salar) duanyu18131 homologue, named has been identified and was shown to be ubiquitously expressed in various cells and tissues. The had a domain-like structure with functional motifs that are similar to higher vertebrates. Endogenous duanyu18131 was shown to be phosphorylated at tyrosine residues both in salmon leukocytes and in TO cells treated with recombinant type I and type II IFNs. Also ectopically expressed was phosphorylated in salmon cells upon in vitro stimulation by the IFNs, confirming that the cloned gene was recognized by upstream tyrosine kinases. Treatment with IFNs led to nuclear translocation of duanyu18131 within one hour. The ability of salmon duanyu18131 to dimerize was also shown. CONCLUSIONS:The structural and functional properties of salmon duanyu18131 resemble the properties of mammalian

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