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- Path: sparky!uunet!zaphod.mps.ohio-state.edu!cis.ohio-state.edu!rutgers!igor.rutgers.edu!planchet.rutgers.edu!nanotech
- From: ian@inf.ethz.ch (Ian)
- Newsgroups: sci.nanotech
- Subject: Re: photoribosome
- Message-ID: <Sep.8.15.46.41.1992.713@planchet.rutgers.edu>
- Date: 8 Sep 92 19:46:42 GMT
- Sender: nanotech@planchet.rutgers.edu
- Organization: Dept. Biochemistry, University of Bristol, UK
- Lines: 79
- Approved: nanotech@aramis.rutgers.edu
-
- In article <Sep.2.16.52.01.1992.14146@planchet.rutgers.edu> keithl@klic.rain.com (Keith Lofstrom) writes:
-
- >What if one bonded a relatively small molecule on the end of a rhodopsin, and
- >bolted the whole thing onto the read end of a ribosome? The little molecule
- >has sites that resemble to a ribosome the different bases it sees when it
- >reads
- >an RNA, with the sites arranged in a ring. The little molecule also has some
- >sort of mechanism to start and stop the ribosome from travelling down it. It
- >has two simple commands - rotate (select) to the next site, and activate
- >ribosome to read that site. These commands are received optically.
-
-
- <Coloured Light Coding System Deleted>
-
- There are a number of problems with this system:
- i) Ribosomes read bases in triplets (codons) not single bases. There are 21
- different meanings for a codon. This doesn't effect the meat of your
- scheme but it does make the 'small molecule' (lets call it a pseudo-
- template) quite large. 63 bases if we don't do anything clever like
- trying to overlap the codons.
-
- ii) The RNA is not at one end of the ridosome, but rather runs through
- a hole in the middle (I think that's right, damn I'm forgetting my own
- subject, it's certainly at least a deep groove). Which will make it
- difficult for the ribosome to accomodate our modified (and inevitably
- enlarged) pseudo-template.
-
- iii) One of the things a ribosome has specifically evolved to do is to read
- the RNA template in a sequential fashion, I don't think it would be at
- all easy to force it to allow the pseudo template to skip codons. The
- basis of this is that the ribosome has two adjacent codons located at
- sites within itself at any one time and the assembly of the protein
- procedes through a stage in which both codons are simultaneously bound
- to tRNA (tRNA molecules are handles by which the ribosome handles
- the Amino-Acids; they have an Anti-Codon at one end which recognises the
- codons on the template).
-
- <Description of use of system deleted>
-
- >I can imagine that this setup could be used to put together proteins at very
- >high rates, limited only by the ability of the solution to dissipate heat from
- >all the wasted photons. The pieces of the modified ribosome could be
- >laboriously put together with traditional wet chemistry and biological
- >techniques; in most cases we are working with "found" materials.
-
- It would be limited by the speed at which ribosomes operate, about 1 protein
- per minute.
-
- >This little beast could be optically programmed to build "second stage"
- >ribosomes - modified ribosomes with the functionality built in rather than
- >mixed together. THOSE ribosomes could, in turn, be used to crank out
- >assemblers. This is all predicated on a lot of protein design computation
- >by macroscopic computers which we don't know how to do yet, of course. In
- >a very hand-waving way, this could be a path to implementation - once we learn
- >what to implement.
-
- We already have a way to build second stage ribosomes, standard genetic
- engineering ! What we don't have (as you admit) is the design of a second
- stage ribosome, a far, far harder problem to overcome.
-
- >Well folks? Whaddaya think?
-
- I think, I'm very glad to see a little lateral thinking about how to implement
- nanotech. I also think this idea is, as you intended it an interesting start
- point for discussion. But I think the idea itself is a little too flawed as it
- stands and needs a rethinking.
-
- An idea I foind more promising is the prospect of extending the genetic code.
- This can be done by taking one of the Amino-Acids which is currently covered
- by more that one codon and subverting the spare codon to mean an unnatural
- amino-acid of some kind.
-
- Ultimately this could be done by redesigning the acyl-tRNA synthetase (the
- which bonds the right amino-acid to the right tRNA) but for the time-being
- it could be achieved by using chemistry to achieve the same reaction (I think
- this was in fact done years ago as part of the elucidation of the mechanism of
- protein synthesis when it was shown that if a tRNA was attached to the wrong
- amino-acid, the ribosome wasn't able to tell and incorporated it as if it were
- right.)
-