Some cool silicon biology to add to the toolbox. Now you can tag proteins by using a nonsense codon that codes for a fluorescent amino acid-tRNA. This technique and similar ones could easily revolutionize cellular tracking of protein trafficking.
This entry was posted on Sunday, July 2nd, 2006 at 4:33 pm by Neville Sanjana and is filed under Biophysics, Genetics and molecular, Methods and techniques. You can follow any responses to this entry through the RSS 2.0 feed. You can leave a response, or trackback from your own site.
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July 20th, 2006 at 8:35 pm
Yeah it’s just too bad that amber (TAG) is a stop codon – that means that this amino acid would lead to unnatural read-through of stop codons in the whole lot of proteins that use amber for their termination sequence. The yeast are (apparently) robust enough in the scheme of things though – they didn’t report any prion-like aggregates.
On the other hand, we could engineer an organism that doesn’t use amber for a stop codon (why is it that we need multiple stop codons anyway)?
July 21st, 2006 at 10:12 am
Probabilistically, you’re likely to stop within a few dozen codons’ worth of DNA anyway, given that the two remaining stop codons are 3% of the codons. And the polyadenylation sequence is also likely to halt transcription at the appropriate point, making it so that there is not much more to the mRNA in any case.