A modular zinc finger adaptor accelerates the covalent linkage of proteins at specific locations on DNA nanoscaffolds

Eiji Nakata, Huyen Dinh, Tien Ngo Anh, Masayuki Saimura, Takashi Morii

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Abstract

A modular adaptor consisting of a sequence-specific DNA binding zinc finger protein and a self-ligating protein-tag was developed to expedite efficient formation of a covalent linkage between an individual protein molecule and the programmed address modified with a tag-substrate on the DNA nanostructure.
Original languageEnglish
JournalChemical Communications
Volume51
Issue number6
Pages (from-to)1016-1019
Number of pages4
ISSN1359-7345
DOIs
Publication statusPublished - 2015
Externally publishedYes

Keywords

  • CHEMISTRY,
  • NANOSTRUCTURES
  • ORIGAMI
  • NANOTECHNOLOGY
  • REACTIVITY
  • MOLECULES
  • SCAFFOLDS
  • COMPLEX
  • Chemistry (all)
  • Catalysis
  • Ceramics and Composites
  • Electronic, Optical and Magnetic Materials
  • Surfaces, Coatings and Films
  • Materials Chemistry
  • Metals and Alloys
  • Medicine (all)
  • basic leucine zipper transcription factor
  • DNA binding protein
  • molecular scaffold
  • oligodeoxynucleotide
  • zinc finger protein
  • DNA
  • nanomaterial
  • signal transducing adaptor protein
  • Article
  • binding kinetics
  • binding site
  • complex formation
  • covalent bond
  • crystal structure
  • dissociation constant
  • DNA binding
  • DNA hybridization
  • DNA protein complex
  • DNA sequence
  • environmental temperature
  • hybridization
  • in vitro study
  • nucleotide sequence
  • polyacrylamide gel electrophoresis
  • protein DNA interaction
  • static electricity
  • atomic force microscopy
  • chemistry
  • metabolism
  • Adaptor Proteins, Signal Transducing
  • DNA-Binding Proteins
  • Microscopy, Atomic Force
  • Nanostructures
  • Zinc Fingers

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