Developing a codon optimization method for improved expression of recombinant proteins in actinobacteria.

ABSTRACT: Codon optimization by synonymous substitution is widely used for recombinant protein expression. Recent studies have investigated sequence features for codon optimization based on large-scale expression analyses. However, these studies have been limited to common host organisms such as Escherichia coli. Here, we develop a codon optimization method for Rhodococcus erythropolis, a gram-positive GC-rich actinobacterium attracting attention as an alternative host organism. We evaluate the recombinant protein expression of 204 genes in R. erythropolis with the same plasmid vector. The statistical analysis of these expression data reveals that the mRNA folding energy at 5' regions as well as the codon frequency are important sequence features for codon optimization. Intriguingly, other sequence

SUBMITTER: Saito Y 

PROVIDER: S-EPMC6554278 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature