Photomodulation of protein trans-splicing through backbone photocaging of the DnaE split intein

Luis Berrade, Youngeun Kwon, Julio A. Camarero

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

Abstract

(Figure Presented) Lightly spliced inteins: A novel strategy to modulate the assembly and trans-splicing activity of the Ssp DnaE split intein was achieved by introducing two photolabile protecting groups onto the backbone of the C-intein polypeptide. This modification was not only able to efficiently block the trans-splicing activity, but also reduce significantly the binding affinity constant between the Cand N-intein fragments. The original activity of the wildtype split intein could be fully recovered by brief exposure to UV light.

Original languageEnglish
Pages (from-to)1368-1372
Number of pages5
JournalChemBioChem
Volume11
Issue number10
DOIs
StatePublished - 5 Jul 2010

Keywords

  • Biotechnology
  • Peptides
  • Photolysis
  • Proteins
  • Recognition

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