Proteins in E. coli coexpressed with recombinant proteins?

Emir ekhatipo at NOSPAMmidway.uchicago.edu
Tue Jan 23 13:18:08 EST 2001


Does anybody have a RecA _deletion_ strain then? Any references on companies
or labs will be much appreciated.

The idea of inactive RecA is good, though it hardly explains why expression
of WT RecA would be induced upon induction of the recombinant protein. Thus,
more likely, as Bob responded me by email, that 34kDa unknown protein could
be one of the stress response proteins that happen to crossreact with the
antibodies against my recombinant protein. However, if RecA can be
considered as a member of the stress response group (?), the 38kDa RecA
(minus whatever deletion) could be a good candidate. Any comments on that?

-Emir



"Michael R. Thompson" <Mike.Thompson at nrc.ca> wrote in message
news:S%hb6.205$%b1.3080256 at tomcat.sk.sympatico.ca...
> Hi Emir,
>
> Do you know what the RecA mutation is in the BLR strain? If it is due to a
> point mutation or partial deletion in the RecA gene, it is possible that
you
> are getting some cross-reacting native RecA protein product, albeit
> inactive.
>
> Regards, Mike.
>
>
> Emir wrote in message ...
> >Hi,
> >I was wondering if anything is known about the indigenous E.coli (or
other
> >bacterial) proteins that are expressed in response to expression of
> >(poisonous) recombinant proteins.
> >
> >Here's my case. I am expressing a 6his-tagged yeast DNA-binding protein
in
> >E. coli (BLR, a RecA- strain) from a T7 promoter-driven expression vector
> >(pET-11). The protein is a homologue of RecA <SNIP>
>
>







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