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The ethylene-forming enzyme (EFE) from  Pseudomonas syringae  catalyzes the synthesis of ethylene which can be easily detected in the headspace of closed cultures. A synthetic codon-optimized gene encoding N-terminal His-tagged EFE (EFEh) was expressed in  Synechocystis  sp. PCC 6803 ( Synechocystis ) and  Escherichia coli  ( E. coli ) under the control of diverse promoters in a self-replicating broad host-range plasmid. Ethylene synthesis was stably maintained in both organisms in contrast to earlier work in  Synechococcus elongatus  PCC 7942. The rate of ethylene accumulation was used as a reporter for protein expression in order to assess promoter strength and inducibility with the different expression systems. Several metal-inducible cyanobacterial promoters did not function in  E. coli  but were well-regulated in cyanobacteria, albeit at a low level of expression. The  E. coli  promoter P trc  resulted in constitutive expression in cyanobacteria regardless of whether IPTG was added or not. In contrast, a Lac promoter variant, P A1lacO-1 , induced EFE-expression in  Synechocystis  at a level of expression as high as the Trc promoter and allowed a fine level of IPTG-dependent regulation of protein-expression. The regulation was tight at low cell density and became more relaxed in more dense cultures. A synthetic quorum-sensing promoter system was also constructed and shown to function well in  E. coli , however, only a very low level of EFE-activity was observed in  Synechocystis , independent of cell density.

Ethylene Synthesis and Regulated Expression of Recombinant Protein in Synechocystis sp. PCC 6803