Activity restored by mixing recombinant domains?
svetlov at oncology.wisc.edu
Tue Oct 28 10:09:37 EST 1997
In article <lloyd.graham-2908560305100001 at tastiger.dbe.csiro.au>,
lloyd.graham at molsci.csiro.au (Lloyd Graham) wrote:
> Greetings all,
> I'm looking for any precedents where the domains of a monofunctional
> enzyme have been expressed separately as inactive proteins, but when mixed
> together they associate to form a complex with significant enzymatic
Although I'm not sure that procaryal RNA polymerase squares well with your
understanding of "monofunctional" enzyme, I suggest looking up the paper
Structural modules of the large subunits of RNA polymerase. Introducing
archaebacterial and chloroplast split sites in the beta and beta' subunits of
Escherichia coli RNA polymerase. J Biol Chem 1996 Nov 1;271(44):27969-27974
by Severinov K. et al.
In this work beta and beta' subunits were expressed in bacteria, split in 2
fragments each (along the archeabacterial A and A', B and B' homolog
boundaries), followed by in vitro reconstitution of the near-native and
enzymatically active RNAP core with alpha subunits.
Hope this helps,
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