Flavohemoglobins, which are widely distributed in prokaryotes and eukaryotes, play key roles in oxygen (O2 ) transport and nitric oxide (·NO) defense. Hmp is the flavohemoglobin of Escherichia coli, and here we report that the translational fusion of Hmp to the N-terminus of heterologous proteins increases their expression in E. coli. The effect required the fusion of the proteins, and was independent of both the O2-binding and catalytic activity of Hmp. Increased expression was at the translational level, likely to be downstream of initiation, and we observed that as little as the first 100 amino acids of Hmp were sufficient to boost protein production. These data demonstrate the potential of Hmp as an N-terminal fusion tag to increase protein yield, and suggest that the utility of bacterial hemoglobins to biotechnology goes beyond their O2 transport and ·NO detoxification capabilities.
|Original language||English (US)|
|State||Published - Feb 2022|
All Science Journal Classification (ASJC) codes
- Microbiology (medical)
- Bacterial hemoglobin
- N-terminal tag
- Nitric oxide