Re: [DIYbio] Re: Exocytosis in Bacteria

A problem you'll have here is throughput. While it's possible to get
some proteins (some!) to export by hijacking existing signals, the
throughput of these systems tends to be low, or inconsistent.

It's easier to get things to the periplasmic space, because the
transport systems for that are homologous to those used by G+ bacteria.
From there, you can do periplasmic rupture easily enough to release
somewhat low-contamination protein.

But, overall, it's not too rosy. This is something I hit a wall with
when researching IndieBB, because the colicinV operon is *mostly
transport proteins* and I wanted to instead re-use a generalised export
system used by cells for everything else, so I could have "world's
smallest selection cassette"... ugh, not really.

On 06/02/15 12:58, Filip Hasecke wrote:
> http://wolfson.huji.ac.il/expression/local/bacteria/Recombinant%20protein%20secretion%20in%20Escherichia%20coli-2005.pdf
>
> There is a big table in this document showing the used signal and the
> resulting cellular localization of the recombinant protein and a link to
> a publication. There are also a lot of signals resulting in the
> secretion of the peptide (localization = "medium").
>
> -Filip
>
> 2015-02-06 12:26 GMT+01:00 Mega [Andreas Stuermer]
> <masterstorm123@gmail.com <mailto:masterstorm123@gmail.com>>:
>
> "e coli signal peptide "
>
> may also be a good keyword.
>
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