Translational Fusion to Hmp Improves Heterologous Protein Expression.

TitleTranslational Fusion to Hmp Improves Heterologous Protein Expression.
Publication TypeJournal Article
Year of Publication2022
AuthorsWan, X, A Link, J, Brynildsen, MP
JournalMicroorganisms
Volume10
Issue2
Date Published2022/02/04
ISSN2076-2607
Abstract

Flavohemoglobins, which are widely distributed in prokaryotes and eukaryotes, play key roles in oxygen (O) transport and nitric oxide (·NO) defense. Hmp is the flavohemoglobin of , and here we report that the translational fusion of Hmp to the N-terminus of heterologous proteins increases their expression in . The effect required the fusion of the proteins, and was independent of both the O-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 O transport and ·NO detoxification capabilities.

DOI10.3390/microorganisms10020358
Alternate JournalMicroorganisms
PubMed ID35208816
PubMed Central IDPMC8879370
Grant ListNA / / Focused Research Team Award, Princeton SEAS, Helen Shipley Hunt *71 /