Journal
CELL
Volume 159, Issue 3, Pages 635-646Publisher
CELL PRESS
DOI: 10.1016/j.cell.2014.09.039
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Funding
- Dutch Cancer Society (KWF)
- UCSF Center for Systems and Synthetic Biology
- NIH Office of The Director (OD)
- National Institute of Dental & Craniofacial Research (NIDCR)
- NIH P50 [GM081879, GM102706]
- NIH Director's Early Independence Award [GM081879]
- NIH R01 [DA036858]
- NIH U01 [CA168370]
- Leukemia and Lymphoma Society
- Howard Hughes Medical Institute
- [GM38499]
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Signals in many biological processes can be amplified by recruiting multiple copies of regulatory proteins to a site of action. Harnessing this principle, we have developed a protein scaffold, a repeating peptide array termed SunTag, which can recruit multiple copies of an antibody-fusion protein. We show that the SunTag can recruit up to 24 copies of GFP, thereby enabling long-term imaging of single protein molecules in living cells. We also use the SunTag to create a potent synthetic transcription factor by recruiting multiple copies of a transcriptional activation domain to a nuclease-deficient CRISPR/Cas9 protein and demonstrate strong activation of endogenous gene expression and re-engineered cell behavior with this system. Thus, the SunTag provides a versatile platform for multimerizing proteins on a target protein scaffold and is likely to have many applications in imaging and controlling biological outputs.
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