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Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea

In Archaea the two major modes of DNA packaging are wrapping by histone proteins or bending by architectural non-histone proteins. To supplement our knowledge about the binding mode of the different DNA-bending proteins observed across the three domains of life, we present here the first model of a...

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Autores principales: Paquet, Françoise, Delalande, Olivier, Goffinont, Stephane, Culard, Françoise, Loth, Karine, Asseline, Ulysse, Castaing, Bertrand, Landon, Celine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3928310/
https://www.ncbi.nlm.nih.gov/pubmed/24558431
http://dx.doi.org/10.1371/journal.pone.0088809
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author Paquet, Françoise
Delalande, Olivier
Goffinont, Stephane
Culard, Françoise
Loth, Karine
Asseline, Ulysse
Castaing, Bertrand
Landon, Celine
author_facet Paquet, Françoise
Delalande, Olivier
Goffinont, Stephane
Culard, Françoise
Loth, Karine
Asseline, Ulysse
Castaing, Bertrand
Landon, Celine
author_sort Paquet, Françoise
collection PubMed
description In Archaea the two major modes of DNA packaging are wrapping by histone proteins or bending by architectural non-histone proteins. To supplement our knowledge about the binding mode of the different DNA-bending proteins observed across the three domains of life, we present here the first model of a complex in which the monomeric Methanogen Chromosomal protein 1 (MC1) from Euryarchaea binds to the concave side of a strongly bent DNA. In laboratory growth conditions MC1 is the most abundant architectural protein present in Methanosarcina thermophila CHTI55. Like most proteins that strongly bend DNA, MC1 is known to bind in the minor groove. Interaction areas for MC1 and DNA were mapped by Nuclear Magnetic Resonance (NMR) data. The polarity of protein binding was determined using paramagnetic probes attached to the DNA. The first structural model of the DNA-MC1 complex we propose here was obtained by two complementary docking approaches and is in good agreement with the experimental data previously provided by electron microscopy and biochemistry. Residues essential to DNA-binding and -bending were highlighted and confirmed by site-directed mutagenesis. It was found that the Arg25 side-chain was essential to neutralize the negative charge of two phosphates that come very close in response to a dramatic curvature of the DNA.
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spelling pubmed-39283102014-02-20 Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea Paquet, Françoise Delalande, Olivier Goffinont, Stephane Culard, Françoise Loth, Karine Asseline, Ulysse Castaing, Bertrand Landon, Celine PLoS One Research Article In Archaea the two major modes of DNA packaging are wrapping by histone proteins or bending by architectural non-histone proteins. To supplement our knowledge about the binding mode of the different DNA-bending proteins observed across the three domains of life, we present here the first model of a complex in which the monomeric Methanogen Chromosomal protein 1 (MC1) from Euryarchaea binds to the concave side of a strongly bent DNA. In laboratory growth conditions MC1 is the most abundant architectural protein present in Methanosarcina thermophila CHTI55. Like most proteins that strongly bend DNA, MC1 is known to bind in the minor groove. Interaction areas for MC1 and DNA were mapped by Nuclear Magnetic Resonance (NMR) data. The polarity of protein binding was determined using paramagnetic probes attached to the DNA. The first structural model of the DNA-MC1 complex we propose here was obtained by two complementary docking approaches and is in good agreement with the experimental data previously provided by electron microscopy and biochemistry. Residues essential to DNA-binding and -bending were highlighted and confirmed by site-directed mutagenesis. It was found that the Arg25 side-chain was essential to neutralize the negative charge of two phosphates that come very close in response to a dramatic curvature of the DNA. Public Library of Science 2014-02-18 /pmc/articles/PMC3928310/ /pubmed/24558431 http://dx.doi.org/10.1371/journal.pone.0088809 Text en © 2014 Paquet et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Paquet, Françoise
Delalande, Olivier
Goffinont, Stephane
Culard, Françoise
Loth, Karine
Asseline, Ulysse
Castaing, Bertrand
Landon, Celine
Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea
title Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea
title_full Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea
title_fullStr Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea
title_full_unstemmed Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea
title_short Model of a DNA-Protein Complex of the Architectural Monomeric Protein MC1 from Euryarchaea
title_sort model of a dna-protein complex of the architectural monomeric protein mc1 from euryarchaea
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3928310/
https://www.ncbi.nlm.nih.gov/pubmed/24558431
http://dx.doi.org/10.1371/journal.pone.0088809
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