Activity restored by mixing recombinant domains?
lloyd.graham at molsci.csiro.au
Thu Oct 30 17:39:19 EST 1997
I began this thread by writing:
> 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
> activity. If anybody can provide instances where purified inactive domains
> complement in vitro, I would be very grateful.
Thanks for all the replies to date, and here is some feedback on them:
* RNAP large subunits... Yes, this is a good one.
* alpha peptide of beta-galactosidase... Sorry, the alpha peptide is too
short (39-50 aa) to be a true domain, and the 3D structure confirms that
it doesn't adopt a globular fold in the intact protein.
* ATCase from E. coli... Would be a good one if the fragments had
corresponded to the two domains but (as the contributor acknowledged) this
was not the case.
There must *surely* be several clean-cut examples of this entirely
expected phenomenon in the literature, but where are they?
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