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Although there are 64 ways of combining four letters, only 61 codons are used to encode the 20 amino acids found in nature. This means that some of the codons encode the same amino acid – a phenomenon called redundancy. The three combinations left over, UAG, UAA and UGA, act like a full stop or period – telling the ribosome to terminate the process at that point. When this happens, rather than an amino acid getting added to the chain, a release factor binds and triggers the release of the peptide, so that it can be folded and processed into a protein.
A team of synthetic biologists led by Farren Isaacs at Yale University have now fundamentally rewritten these rules. They took Escherichia coli cells and replaced all of their UAG stop codons with UAAs. They also deleted the instructions for making the release factor that usually binds to UAG, rendering UAG meaningless.
Next they set about assigning UAG a new meaning, by designing molecules called tRNAs and accompanying enzymes that would attach an unnatural amino acid – fed to the cell – whenever they spotted this codon. Many such amino acids have been designed, but they can't usually be processed by living organisms and incorporated into their proteins. By reintroducing UAGs at specific locations within genes, the team were able to add unnatural amino acids into proteins at will.
"We now have an organism that has a new code, and we can reliably and efficiently open up the chemical diversity of proteins by introducing a whole new array of amino acids using UAG as the codon," says Isaacs.
"It has great potential for the future to not just replace one here and there, but to replace loads of them and have completely new types of biopolymers made in cells. It's a first step down the road to a new biology," he says.
"[Isaac's team] argue that they can recode living existing genomes quickly and efficiently which can increase biological diversity."
What's more, there's little threat of recoded E. coli swapping genes with its natural counterpart, were GROs ever to escape into the wild. Reassigned stop codons would be read as normal stop codons in natural cells, resulting in the premature termination of protein production. Preliminary studies also suggest that GROs cannot grow in the absence of the unnatural amino acid they've been designed to incorporate – adding another level of security.
"This is a big step forward," says Steve Benner of the Foundation for Applied Molecular Evolution in Gainesville, Florida. "Once you have a cell that's able to handle your concept of DNA and your concept of amino acids, then you are opening up an entirely new field of science."
What's more, there's little threat of recoded E. coli swapping genes with its natural counterpart, were GROs ever to escape into the wild. Reassigned stop codons would be read as normal stop codons in natural cells, resulting in the premature termination of protein production. Preliminary studies also suggest that GROs cannot grow in the absence of the unnatural amino acid they've been designed to incorporate – adding another level of security.
Panic2k11
reply to post by CitizenJack
Life is not static and we still do not understand its workings to establish clear safety rules, from viral cross genetic transfer to mutations to the way bacteria share genetically information the door to something going wrong is very large.
Moving this industry off world (for stats) would be a great boost for economic sustainability of colonization and even help extraterrestrial industry, mining and terraforming,..
edit on 17-10-2013 by Panic2k11 because: (no reason given)
CitizenJack
reply to post by Bedlam
I did not know that. That makes a lot of sense to build in a self correcting error , nature is a pretty efficient mechanism. Thanks for that tidbit I find it very interesting and wonder how this applies to the research.edit on 17-10-2013 by CitizenJack because: (no reason given)edit on 17-10-2013 by CitizenJack because: (no reason given)