 Hi, welcome to VB Video Abstract. I'm Professor Sangyun Shim of Korea University. I would like to talk about our new recombinant tagging system for the protein expression between the ribosomal frame shifting and green fluorescence protein. Many protein detection and tagging methods have been developed to determine recombinant protein expression levels. In particular, green fluorescence protein, GFP, is a versatile fluorescence protein marker. Since the GFP fluorescence signal is correlated to protein concentration, GFP can be used as a quantitative tool for real-time identification of gene expression. However, because our protein world is pressed in a GFP-fields form, there was a substantial metabolic burden on host cells and decreased in protein activity. To overcome these difficulties, we have employed program the minus 1 ribosomal frame shifting, minus 1 RFS. Minus 1 RFS is an essential common strategy adopted by many viruses, which regulates the relative expression of proteins encoded in two overlapping translational reading frames. Minus 1 RFS is a change in the translational reading frame such that the curtains start one nucleotide upstream from the original position in the messenger RNA sequence. We were interested in the use of minus 1 RFS as an embodied device to quantitatively manipulate protein expression and tagging. In other expression systems, the expression of fusion protein with EGFP led to decreased expression of the target protein. We designed new expression vectors based on our strategy in which a stop codon and RNA-6 element for minus 1 RFS are between the target and enhanced GFP genes. Due to the minus 1 RFS, both intact and fused forms of target proteins are expressed simultaneously at a predetermined ratio. Since minus 1 RFS occurs continuously at constant efficiency, quantitation of EGFP in the fusion protein allows for the calculation of concentrations of unmodified target protein based on this ratio. bulk protein synthesis is a metabolic burden on the host cell, though in our strategy, because only a small portion of the recombinant protein include EGFP fusion, most of the cell's energy can be spent on producing the target protein. Here we validated this process using Grutachian S-transferase GST as a target protein and minus 1 RFS signals. By using minus 1 RFS system, we had three-fold higher GST activity than that of a fusion system. This limited tagging would be valuable for the real-time monitoring of a protein expression when optimizing the expression condition for a new protein and in monitoring large-scale bioprocesses. The more details are in biotechnology and bioengineering journal. Thank you.