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 aris : Proteins are amazingly promiscuous, mixing and matching in a tango of life and then splitting up and reforming in a different combination, scientists have found.
In two studies published on Thursday, their findings represent big step forward in the new science of proteomics - the study of how proteins work. Proteomics flows from genomics, the study of the gene, and is viewed by many as potentially the most lucrative prize in all biotechnology, Genes control proteins, the molecules that comprise living tissue, maintain it or destroy it.
Understanding a proteome how an organism's set of proteins work and how they ineract would be a breakthrough in pharmaceuticals. It would open the door to new treatments that would target specific genes to cure or prevent complex diseases, or tailor drugs to an individual's needs.
Two teams, one led by GiulioSuperti - Furga of cellzome AG and the European Molecular Biology Laboratory in Heidelberg, and another led by Mike Tyers of the Mount Sinai Hospital and University of Toronto, Canada have started work on building the proteomic library. In a painstaking undertaking, they catalogued many of the proteins in yeast (saccharomyces cerevisiae), a species that is a favourite subject for laboratory research.
Even through yeast is only a single-celled organism, it shares many of the same protein functions as more sophisticated life forms, including the human being. Reporting in Thursday's issue of Nature, the British science journal, the Superti-Furga team says they have identified 1,440 separate proteins within 232, protein clusters in yeast, while the Tyres group says they have identified 1,578 proteins.
The most valuable insight is the complexity of interaction between proteins as they build and sustain cellular life. About 85 percent of the proteins that have been identified so far link up with others to perform various functions, the terms found.
The discovery has big implications for drug research, as many drugs today are aimed at only a single protein. It now seems clear that proteins have multiple roles. So if one protein is affected by a drug, that could have a knock-on effect on other functions that may have nothing to do with the ailment. "Proteomic studies such as these have generated a huge volume of exciting data," Anuj Kumar and Michael Snyder, of Yale University's department of molecular, cellular and developmental biology, said in a commentary.
They cautioned, however, that much remained to be learned before the proteome of even a simple organism such as yeast is unraveled, let alone the protein blueprint of a complex, multicelled organism such as a laboratory mouse. They estimated that the yeast proteome probably has around 30,000 protein interactions, of which at most only 11,000 have so far been discovered. The scientists used a molecular form of fishing to share their proteins.
They attached DNA tags to hundreds of proteins and sat back and watched as these proteins teamed up with other proteins, often forming complexes. At that point, the tagged protein was fished out, taking the complex with it.
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