CHAMPAIGN, Ill. Researchers report that they are the first to show in molecular detail how one gene evolved two competing functions that eventually split up via gene duplication to pursue their separate destinies.
The study, in the Proceedings of the National Academy of Sciences, validates a decades-old hypothesis about a key mechanism of evolution. The study also confirms the ancestry of a family of "antifreeze proteins" that helps the Antarctic eelpout survive in the frigid waters of the Southern Ocean.
"I'm always asking the question of where these antifreeze proteins come from," said University of Illinois animal biology professor Christina Cheng, who has spent three decades studying the genetic adaptations that enable Antarctic fish to survive in one of the coldest zones on the planet. "The cell usually does not create new proteins from scratch."
Scientists have known since 2001 that the sequence of genes coding for a family of antifreeze proteins (known as AFP III) was very similar to part of a sequence of a gene that codes for a cellular enzyme in humans. Since Antarctic fish also produce this enzyme, sialic acid synthase (SAS), it was thought that the genes for these antifreeze proteins had somehow evolved from a duplicate copy of the SAS gene. But no study had shown how this happened with solid experimental data.
Cheng and her colleagues at the Chinese Academy of Sciences began by comparing the sequences of the SAS and AFP III genes. There are two SAS genes in fish: SAS-A and SAS-B. The researchers confirmed that the AFP III genes contain sequences that are most similar to those in a region of SAS-B.
They also found a sequence in the SAS-B gene that, when translated into a new protein, could with a few modifications direct the cell to secrete the protein. This slightly modifie
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University of Illinois at Urbana-Champaign