Communication

The High ZnII Affinity of the Tetracysteine Tag Affects Its Fluorescent Labeling with Biarsenicals

  1. Adam Pomorski,
  2. Jacek Otlewski Prof.,
  3. Artur Krężel Dr.

Article first published online: 3 MAY 2010

DOI: 10.1002/cbic.200900768

Issue

ChemBioChem

ChemBioChem

Volume 11, Issue 9, pages 1214–1218, June 14, 2010

Additional Information

How to Cite

Pomorski, A., Otlewski, J. and Krężel, A. (2010), The High ZnII Affinity of the Tetracysteine Tag Affects Its Fluorescent Labeling with Biarsenicals. ChemBioChem, 11: 1214–1218. doi: 10.1002/cbic.200900768

Author Information

  1. Laboratory of Protein Engineering, Faculty of Biotechnology, University of Wrocław ul. Tamka 2, 50-137 Wrocław (Poland), Fax: (+48) 71-375-2608

Publication History

  1. Issue published online: 7 JUN 2010
  2. Article first published online: 3 MAY 2010
  3. Manuscript Received: 16 DEC 2009

Funded by

  • Polish Ministry of Science and Higher Education. Grant Number: N N302 137735
  • Foundation for Polish Science. Grant Number: HOM/2008/8B

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Keywords:

  • biarsenical probe;
  • FIAsH-EDT2;
  • fluorescence;
  • tetracysteine tag;
  • zinc
Thumbnail image of graphical abstract

Zinc sink: CCPGCC motifs added to a protein sequence provide a favorable environment for ZnII coordination. This interaction reduces the binding of biarsenicals to the tetracysteine tag. Zinc's high affinity for this motif can affect the zinc pool in a eukaryotic system if a protein containing the motif is expressed at high concentration.

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