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Abstract
The paired box 6 (Pax6) gene encodes a transcription factor essential for eye development in a wide range of animal lineages. Here we describe the cloning and characterization of Pax6 gene from the blind hydrothermal vent tubeworm Ridgeia piscesae (RpPax6). The deduced RpPax6 protein shares extensive sequence identity with Pax6 proteins from other species and contains both the paired domain and a complete homeodomain. Phylogenetic analysis indicates that it clusters with the corresponding sequence from the closely related species Platynereis dumerilii (P. dumerilii) of Annelida. Luciferase reporter assay indicate that RpPax6 protein suppresses the transcription of sine oculis (so) in D. melanogaster, interfering with the C-terminal of RpPax6. Taking advantage of Drosophila model, we show that RpPax6 expression is not able to rescue small eye phenotype of ey2 mutant, only to cause a more severe headless phenotype. In addition, RpPax6 expression induced apoptosis and inhibition of apoptosis can partially rescue RpPax6-induced headless phenotype. We provide evidence RpPax6 plays at least two roles: it blocks the expression of later-acting transcription factors in the eye development cascade, and it promotes cell apoptosis. Our results indicate alternation of the Pax6 function may be one of the possible causes that lead the eye absence in vestimentiferan tubeworms.
Highlights
Members of the paired box (Pax) gene family encode transcription factors that are characterized by a DNA-binding paired domain of 128 amino acids located at the amino terminal end [1]
Our results suggest that functional alternation of RpPax6 may be involved in the eye absence in vestimentiferan tubeworms
Amino acids sequence alignment of RpPax6 and the pax6 from different species reveal that the paired domains and homeodomains are highly conserved (Fig 1)
Summary
Members of the paired box (Pax) gene family encode transcription factors that are characterized by a DNA-binding paired domain of 128 amino acids located at the amino terminal end [1]. Some Pax proteins contain a partial or complete paired-type homeodomain and/or an octapeptide motif. Members of the Pax gene family are involved in the regulation of wide range of developmental processes, including segmentation and organogenesis [2, 3]. Pax is one of the well-characterized Pax genes which plays critical role in eye development in diverse animal lineages. It contains both a paired and a complete homeodomain. The genomic organization, domain sequences, and function are highly conserved [4, 5]
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