Applications
In 2002, the TAP tag was first used with mass spectrometry in a large-scale approach to systematically analyse the proteomics of yeast by characterizing multiprotein complexes. The study revealed 491 complexes, 257 of them wholly new. The rest were familiar from other research, but now virtually all of them were found to have new components. They drew up a map relating all the protein components functionally in a complex network.
Many other proteomic analyses also involve the use of TAP tag. A research by EMBO (Dziembowski, 2004) identified a new complex required for nuclear pre-mRNA retention and splicing. They have purified a novel trimeric complex composed of 3 other subunits (Snu17p, Bud13p and Pml1p) and find that these subunits are not essential for viability but required for efficient splicing (removal of introns) of pre-mRNA. In 2006, Fleischer et al. systematically identified proteins associated with eukaryotic ribosomal complexes. They used multifaceted mass spectrometry proteomic screens to identify yeast ribosomal complexes and then used TAP tagging to functionally link up all these proteins.
Read more about this topic: Tandem Affinity Purification