Expression of an Anacystis nidulans photolyase gene in Escherichia coli; functional complementation and modified action spectrum of photoreactivation

Photochem Photobiol. 1989 Nov;50(5):633-7. doi: 10.1111/j.1751-1097.1989.tb04319.x.


The Anacystis nidulans photolyase gene inserted in an expression vector plasmid was introduced into Escherichia coli cells and the production of Anacystis photolyase protein was confirmed by reaction with antibodies raised against photolyase purified from A. nidulans cells. The Anacystis photolyase functioned in photoreactivation repair defective E. coli cells. The E. coli transformants exhibited an action spectrum with a maximum around 380 nm similar to that of E. coli photolyase in contrast with the action spectrum of A. nidulans cells which has a maximum at 437 nm. These results indicate that the Anacystis photolyase produced in E. coli cells has enzymatic activity in spite of the apparent lack of its intrinsic 8-hydroxy-5-deazaflavin cofactor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cloning, Molecular
  • Coenzymes
  • Cyanobacteria / enzymology*
  • Cyanobacteria / genetics
  • DNA Repair*
  • Deoxyribodipyrimidine Photo-Lyase / genetics*
  • Deoxyribodipyrimidine Photo-Lyase / metabolism
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Gene Expression*
  • Immunoblotting
  • Lyases / genetics*
  • Molecular Sequence Data
  • Mutation
  • Photochemistry
  • Plasmids
  • Promoter Regions, Genetic
  • Riboflavin / analogs & derivatives
  • Riboflavin / analysis
  • Transformation, Bacterial


  • Coenzymes
  • factor 420
  • Lyases
  • Deoxyribodipyrimidine Photo-Lyase
  • Riboflavin