Flavocytochrome cloned, expression

The success of Chapman and co-workers in expression of flavocytochrome 2 in E. coli [23] is encouraging in its impUcations for future expression of flavoproteins in this host because, in their experience both the flavin and heme groups are incorporated into the recombinant protein. Moreover, the bacterial expression system produces the protein 500-1000 fold more efficiently than the yeast from which it was cloned. The enzyme produced in E. coli, however, lacks the first five amino acid residues at its amino terminus, a result which presumably reflects subtle differences in protein synthesis between the two organisms. 

Saccharomyces cerevisiae is quite commonly used as a host for expression of proteins from cloned genes from yeasts and other organisms. Because flavocytochrome 62 is a yeast enzyme and procedures for isolation of intact enzyme from yeast had already been developed, Reid et al. (143) developed a system for expression of S. cerevisiae flavocy-... 

Several point mutations in the S. cerevisiae flavocytochrome coding sequence have been constructed by oligonucleotide-directed site-specific mutagenesis of the cloned gene (143). The enzyme-coding region was transferred to a plasmid designed both for expression of... 

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