Activity restored by mixing recombinant domains?

colossus... s535290 at aix1.uottawa.ca
Fri Oct 31 13:17:36 EST 1997


Lloyd...I was thinking about this a little bit, and I don't know if this
is exactly what you are looking for, but for instance the yeast SNF1
kinase is inactive. It requires the SNF4 protein in order to be activated.
SNF1 has the catalytic domain whereas the SNF4 kinase is a non-catalytic
subunit. Apparently the SNF4 protein interacts with the pseudo-substrate
site of the SNF1 kinase and frees up the catalytic domain thereby
activating it.

dunno if this will be of any help, 

Ed

> 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. 




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