I'm familiar with the use of alpha-complementation of beta-galactosidase with the pUC alpha-peptide and the M15 lacZ gene product, and would like to hypothetically apply alpha-complementation in other settings with different enzymes. I do have a few questions, but hopefully they are similar enough to all be answered here.
What specifically allows for the non-covalent association between both truncated protein products to form a functional beta-galactosidase? How is beta-galactosidase unique in that separating it into two portions still yields a functional enzyme (in other words, why wouldn't other enzymes remain functional if I split them)?
What other proteins, if any, have been engineered to perform similar alpha-complementation? What steps were taken to accomplish this?
