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Protein delivery using Cys2-His2 zinc-finger domains

Academic Article
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Overview

related to degree

  • Gaj, Thomas, Ph.D. in Chemical Biology, Scripps Research 2007 - 2013

authors

  • Gaj, Thomas
  • Liu, J.
  • Anderson, K. E.
  • Sirk, S. J.
  • Barbas III, Carlos

publication date

  • August 2014

journal

  • ACS Chemical Biology  Journal

abstract

  • The development of new methods for delivering proteins into cells is a central challenge for advancing both basic research and therapeutic applications. We previously reported that zinc-finger nuclease proteins are intrinsically cell-permeable due to the cell-penetrating activity of the Cys2-His2 zinc-finger domain. Here, we demonstrate that genetically fused zinc-finger motifs can transport proteins and enzymes into a wide range of primary and transformed mammalian cell types. We show that zinc-finger domains mediate protein uptake at efficiencies that exceed conventional protein transduction systems and do so without compromising enzyme activity. In addition, we demonstrate that zinc-finger proteins enter cells primarily through macropinocytosis and facilitate high levels of cytosolic delivery. These findings establish zinc-finger proteins as not only useful tools for targeted genome engineering but also effective reagents for protein delivery.

subject areas

  • Amino Acid Sequence
  • Cell Line
  • Cysteine
  • Histidine
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Proteins
  • Zinc Fingers
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Identity

PubMed Central ID

  • PMC4519095

International Standard Serial Number (ISSN)

  • 1554-8929

Digital Object Identifier (DOI)

  • 10.1021/cb500282g

PubMed ID

  • 24936957
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Additional Document Info

start page

  • 1662

end page

  • 1667

volume

  • 9

issue

  • 8

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