What is it about?
Regulation of the nuclease action in artificial nucleases is indispensable for future therapeutic applications. Our research contribute to better understanding of the allosteric effect of the N-terminal sequence on the catalytic C-terminal unit in Colicin E7.
Featured Image
Why is it important?
Artificial nucleases that are presently applied in genome engineering (e.g. FokI nuclease domain fused to zinc finger or TALE proteins, or the CRISPR/Cas9 system) are prone to perform off target cleavages. Even if they are applicable in in vitro experiments, they may be damaged in the cells leading to non-specific cleavages. We are searching for a new nuclease domain, which can be allosterically activated so that any damage of the enzyme should prevent its activity.
Read the Original
This page is a summary of: Fine tuning of the catalytic activity of colicin E7 nuclease domain by systematic N‐terminal mutations, Protein Science, June 2014, Wiley,
DOI: 10.1002/pro.2497.
You can read the full text:
Contributors
The following have contributed to this page
