Part:BBa_K4427003

El222

We have used the native light-sensitive DNA-binding protein (EL222) of the Marine bacterium Erythrobacter litoralis HTCC2594 to construct a regulatory primer system (bidirectional regulation) for blue light induction and inhibition in Escherichia coli.

EL222 is a modular 222-amino acid photosensitive protein, which is composed of an N-terminal photooxygen voltage (LOV) domain and a C-terminal helix-to-helix (HTH) DNA binding domain, and has the characteristics of a LuxR-type DNA binding protein. Upon exposure to blue light (450 nm), the LOV-HTH interaction is released, enabling EL222 to dimerize and bind to DNA. In the dark, EL222 reverses spontaneously because the N-terminal LOV domain inhibits the C-terminal HTH domain from binding to DNA, thereby rapidly inactivating EL222.

The former version of EL222 is BBa_K2332004, and our figure showed that we have more specific result and our EL222's transcriptional efficiency is better than others.

Here are our figures:

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal XhoI site found at 511
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 81
  
• 1000
  COMPATIBLE WITH RFC[1000]