I've been wading my way through journal articles trying to find
something on the expression of cadherins in prokaryotes. Everything I
can find is to do with their expression for structural analysis with
various cadherin domains being expressed as soluble protiens(often
resulting in inclusion bodies) and then purified rather than the full
endo and ecto domains plus TM domain. It is incredibly frustrating.
On the upside - from what I can tell there are no disulphide bonds in
cadherin extracellular domains.
My concern with all this is that unless I'm missing something - there
hasn't really been an attempt to express a functional cadherin in a
prokaryote and we could spend years trying to get it working ourselves
- and we don't have years.
Another, less cool idea, is that we could try and get all the buoyant
bacteria in a solution to congregate - though not adhere - around the
intersection of the two light sources by making those at the
intersection express a chemoattractant -thus going from a homogenous
bacterial suspension to one with a ball of bacteria (that would
disperse at the end of the stimulus).
Its just another idea - and once again it relies on our ability to get
the second light receptor system working.