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

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, w...

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Autores principales: Driessen, Rosalie P. C., Meng, He, Suresh, Gorle, Shahapure, Rajesh, Lanzani, Giovanni, Priyakumar, U Deva, White, Malcolm F., Schiessel, Helmut, van Noort, John, Dame, Remus Th.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3592393/
https://www.ncbi.nlm.nih.gov/pubmed/23155062
http://dx.doi.org/10.1093/nar/gks1053
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author Driessen, Rosalie P. C.
Meng, He
Suresh, Gorle
Shahapure, Rajesh
Lanzani, Giovanni
Priyakumar, U Deva
White, Malcolm F.
Schiessel, Helmut
van Noort, John
Dame, Remus Th.
author_facet Driessen, Rosalie P. C.
Meng, He
Suresh, Gorle
Shahapure, Rajesh
Lanzani, Giovanni
Priyakumar, U Deva
White, Malcolm F.
Schiessel, Helmut
van Noort, John
Dame, Remus Th.
author_sort Driessen, Rosalie P. C.
collection PubMed
description 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.
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spelling pubmed-35923932013-03-08 Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends Driessen, Rosalie P. C. Meng, He Suresh, Gorle Shahapure, Rajesh Lanzani, Giovanni Priyakumar, U Deva White, Malcolm F. Schiessel, Helmut van Noort, John Dame, Remus Th. Nucleic Acids Res Gene Regulation, Chromatin and Epigenetics 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. Oxford University Press 2013-01 2012-11-15 /pmc/articles/PMC3592393/ /pubmed/23155062 http://dx.doi.org/10.1093/nar/gks1053 Text en © The Author(s) 2012. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 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 journals.permissions@oup.com.
spellingShingle Gene Regulation, Chromatin and Epigenetics
Driessen, Rosalie P. C.
Meng, He
Suresh, Gorle
Shahapure, Rajesh
Lanzani, Giovanni
Priyakumar, U Deva
White, Malcolm F.
Schiessel, Helmut
van Noort, John
Dame, Remus Th.
Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends
title Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends
title_full Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends
title_fullStr Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends
title_full_unstemmed Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends
title_short Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends
title_sort crenarchaeal chromatin proteins cren7 and sul7 compact dna by inducing rigid bends
topic Gene Regulation, Chromatin and Epigenetics
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3592393/
https://www.ncbi.nlm.nih.gov/pubmed/23155062
http://dx.doi.org/10.1093/nar/gks1053
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