Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends

Rosalie P.C. Driessen, He Meng, Gorle Suresh, Rajesh Shahapure, Giovanni Lanzani, U. Deva Priyakumar, Malcolm F. White, Helmut Schiessel, John Van Noort, Remus Th Dame

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)196-205
Number of pages10
JournalNucleic acids research
Volume41
Issue number1
DOIs
StatePublished - Jan 2013

ASJC Scopus subject areas

  • Genetics

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