University of MinnesotaMinneapolis 55455Minnesota
Sommese R.F.,University of MinnesotaMinneapolis 55455Minnesota |
Kim K.,University of MinnesotaMinneapolis 55455Minnesota |
Liu M.,Arizona State UniversityTempe 85287Arizona |
Sivaramakrishnan S.,University of MinnesotaMinneapolis 55455Minnesota
Protein Science | Year: 2016
DNA nanostructures have become an important and powerful tool for studying protein function over the last 5 years. One of the challenges, though, has been the development of universal methods for patterning protein complexes on DNA nanostructures. Herein, we present a new approach for labeling DNA nanostructures by functionalizing them with a GFP nanobody. We demonstrate the ability to precisely control protein attachment via our nanobody linker using two enzymatic model systems, namely adenylyl cyclase activity and myosin motility. Finally, we test the power of this attachment method by patterning unpurified, endogenously expressed Arp2/3 protein complex from cell lysate. By bridging DNA nanostructures with a fluorescent protein ubiquitous throughout cell and developmental biology and protein biochemistry, this approach significantly streamlines the application of DNA nanostructures as a programmable scaffold in biological studies. © 2016 The Protein Society.