Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends
MetadataShow full item record
Archaeal chromatin proteins share molecular and functional similarities with both bacterial and eukaryotic chromatin proteins. These proteins play an important role in functionally organizing the genomic DNA into a compact nucleoid. Cren7 and Sul7 are two crenarchaeal nucleoid-associated proteins, which are structurally homologous, but not conserved at the sequence level. Co-crystal structures have shown that these two proteins induce a sharp bend on binding to DNA. In this study, we have investigated the architectural properties of these proteins using atomic force microscopy, molecular dynamics simulations and magnetic tweezers. We demonstrate that Cren7 and Sul7 both compact DNA molecules to a similar extent. Using a theoretical model, we quantify the number of individual proteins bound to the DNA as a function of protein concentration and show that forces up to 3.5 pN do not affect this binding. Moreover, we investigate the flexibility of the bending angle induced by Cren7 and Sul7 and show that the protein-DNA complexes differ in flexibility from analogous bacterial and eukaryotic DNA-bending proteins.
Driessen , R P C , Meng , H , Suresh , G , Shahapure , R , Lanzani , G , Priyakumar , U D , White , M F , Schiessel , H , van Noort , J & Dame , R T 2013 , ' Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends ' , Nucleic Acids Research , vol. 41 , no. 1 , pp. 196-205 . https://doi.org/10.1093/nar/gks1053
Nucleic Acids Research
© The Author(s) 2012. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial reuse, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact email@example.com.
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.