A student isolated GENOMIC DNA known to encode for a protease from Staph aureus
ID: 192258 • Letter: A
Question
A student isolated GENOMIC DNA known to encode for a protease from Staph aureus and expressed it in E. coli and the protein expressed fine and functioned fine. The same student isolated GENOMIC DNA known to encode for a protease from a human fibroblast and expressed that in E. coli and a protein was expressed, BUT the size of the obtained protein was different from the known protease expressed by the fibroblast and it also didn’t function well. There at least TWO major potential reasons for this what are they? One reason is associated with a post-transcriptional process and another reason is associated with a post-translational process.
Explanation / Answer
The post-transcriptional reason should be the intron splicing because the eukaryotic gene which would generally undergo splicing mechanism, if expressed in the prokaryotic system like E. coli would not give functional protein as the prokaryotes do not have splicing mechanism.
The post-translational reason is once the protease is getting translated in fibroblast cells it would undergo trimming so that it will become functional. The same protease if expressed in prokaryotes will not be functional because the enzymes which are needed for trimming will not be there in prokaryotes.
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