Seyed Mohammad Amin Mahdian; Abbasali Raz; Navid Dinparast Djadid; Hamzeh Alipour
Abstract
Background: A given amino acid sequence can be encoded by a huge number of different nucleic acid sequences. These sequences, however, have proved not to be equally useful. The choice of sequence can significantly impact the expression of an encoded protein. Given the importance of protein-coding sequence ...
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Background: A given amino acid sequence can be encoded by a huge number of different nucleic acid sequences. These sequences, however, have proved not to be equally useful. The choice of sequence can significantly impact the expression of an encoded protein. Given the importance of protein-coding sequence and promising industrial and medicinal applications of Clostridium histolyticum collagenase, this study examined the codon optimization of the Col H gene so as to enhance collagenase expression in Escherichia coli (E. coli).
Methods: This is an experimental study in which the CDS of Col H gene was optimized according to the codon usage of E. coli, using Gene Designer software (DNA 2.0).
Results: The results revealed that relative frequency of codon usage in Col H gene was adapted to the most preferred triplets in E. coli in such a way that codon usage bias in E. coli was enhanced after codon optimization. The higher level of collagenase expression was more likely the result of substituting rare codons with optimal codons.
Conclusion: The findings of this study suggest that codon optimization provides a theoretical improvement in Col H gene expression in E. coli. Nevertheless, experimental research is needed to confirm the improvement.
