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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?

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Maybe this review is a good start: ncbi.nlm.nih.gov/pubmed/22070901 –  rwst Sep 17 '12 at 6:58
Two other (free) papers on beta-gal complementation and other split reporter systems: ncbi.nlm.nih.gov/pmc/articles/PMC2835542 ncbi.nlm.nih.gov/pmc/articles/PMC137764 –  rwst Sep 17 '12 at 7:01

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