Our Angewandte paper on giant DNA-enzyme conjugates highlighted on CNRS website

Monday, December 10th 2012

Our Angewandte paper on giant DNA-enzyme conjugates highlighted on CNRS website
10 Dec 2012. Our recent Angewandte paper, entitled "Enhancement and modulation of enzymatic activity through higher-order structural changes of giant DNA-protein multibranch conjugates", has just been highlighted in the CNRS website "En direct des laboratoires de l'institut de Chimie".

You can read the highlight there


Abstract: Conjugating an oligonucleotide to a protein is a widely used strategy to combine the protein function with a recognition ability provided by the short DNA fragment. On the other hand, genomic DNA molecules, due to their extremely large size, have the unique ability to undergo dramatic higher-order structural changes upon addition of compaction/unfolding agents, but the influence of these structural changes on a conjugated protein has never been explored. Here, we describe the first preparation of giant DNA-protein multibranch conjugates and study how regulated higher-order structural changes of DNA can control the protein function. These conjugates are composed of a beta-lactamase enzyme attached to one to four 48.5 kbp λDNA "branches". We show that the presence of giant DNA induces an enhancement of the enzymatic activity, which can be decreased by compaction with spermine and recovered by unfolding with NaCl.

Reference:

Enhancement and modulation of enzymatic activity through higher-order structural changes of giant DNA-protein multibranch conjugates
S. Rudiuk, A. Venancio-Marques, D. Baigl*
Angew. Chem. Int. Ed. 2012, 51, 12694 –12698
- doi : 10.1002/anie.201206962


Damien Baigl

ASAP papers from NATURE
ASAP papers from SCIENCE