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Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone

BACKGROUND: Complexes of nucleosomes, which often occur in the gene promoter areas, are one of the fundamental levels of chromatin organization and thus are important for transcription regulation. Investigating the dynamic structure of a single nucleosome as well as nucleosome complexes is important...

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Autores principales: Ramaswamy, Amutha, Ioshikhes, Ilya
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2216022/
https://www.ncbi.nlm.nih.gov/pubmed/17996059
http://dx.doi.org/10.1186/1472-6807-7-76
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author Ramaswamy, Amutha
Ioshikhes, Ilya
author_facet Ramaswamy, Amutha
Ioshikhes, Ilya
author_sort Ramaswamy, Amutha
collection PubMed
description BACKGROUND: Complexes of nucleosomes, which often occur in the gene promoter areas, are one of the fundamental levels of chromatin organization and thus are important for transcription regulation. Investigating the dynamic structure of a single nucleosome as well as nucleosome complexes is important for understanding transcription within chromatin. In a previous work, we highlighted the influence of histone variants on the functional dynamics of a single nucleosome using normal mode analysis developed by Bahar et al. The present work further analyzes the dynamics of nucleosome complexes (nucleosome oligomers or oligonucleosomes) such as dimer, trimer and tetramer (beads on a string model) with conventional core histones as well as with the H2A.Z histone variant using normal mode analysis. RESULTS: The global dynamics of oligonucleosomes reveal larger amplitude of motion within the nucleosomes that contain the H2A.Z variant with in-planar and out-of-planar fluctuations as the common mode of relaxation. The docking region of H2A.Z and the L1:L1 interactions between H2A.Z monomers of nucleosome (that are responsible for the highly stable nucleosome containing variant H2A.Z-histone) are highly dynamic throughout the first two dynamic modes. CONCLUSION: Dissection of the dynamics of oligonucleosomes discloses in-plane as well as out-of-plane fluctuations as the common mode of relaxation throughout the global motions. The dynamics of individual nucleosomes and the combination of the relaxation mechanisms expressed by the individual nucleosome are quite interesting and highly dependent on the number of nucleosome fragments present in the complexes. Distortions generated by the non-planar dynamics influence the DNA conformation, and hence the histone-DNA interactions significantly alter the dynamics of the DNA. The variant H2A.Z histone is a major source of weaker intra- and inter-molecular correlations resulting in more disordered motions.
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spelling pubmed-22160222008-01-29 Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone Ramaswamy, Amutha Ioshikhes, Ilya BMC Struct Biol Research Article BACKGROUND: Complexes of nucleosomes, which often occur in the gene promoter areas, are one of the fundamental levels of chromatin organization and thus are important for transcription regulation. Investigating the dynamic structure of a single nucleosome as well as nucleosome complexes is important for understanding transcription within chromatin. In a previous work, we highlighted the influence of histone variants on the functional dynamics of a single nucleosome using normal mode analysis developed by Bahar et al. The present work further analyzes the dynamics of nucleosome complexes (nucleosome oligomers or oligonucleosomes) such as dimer, trimer and tetramer (beads on a string model) with conventional core histones as well as with the H2A.Z histone variant using normal mode analysis. RESULTS: The global dynamics of oligonucleosomes reveal larger amplitude of motion within the nucleosomes that contain the H2A.Z variant with in-planar and out-of-planar fluctuations as the common mode of relaxation. The docking region of H2A.Z and the L1:L1 interactions between H2A.Z monomers of nucleosome (that are responsible for the highly stable nucleosome containing variant H2A.Z-histone) are highly dynamic throughout the first two dynamic modes. CONCLUSION: Dissection of the dynamics of oligonucleosomes discloses in-plane as well as out-of-plane fluctuations as the common mode of relaxation throughout the global motions. The dynamics of individual nucleosomes and the combination of the relaxation mechanisms expressed by the individual nucleosome are quite interesting and highly dependent on the number of nucleosome fragments present in the complexes. Distortions generated by the non-planar dynamics influence the DNA conformation, and hence the histone-DNA interactions significantly alter the dynamics of the DNA. The variant H2A.Z histone is a major source of weaker intra- and inter-molecular correlations resulting in more disordered motions. BioMed Central 2007-11-08 /pmc/articles/PMC2216022/ /pubmed/17996059 http://dx.doi.org/10.1186/1472-6807-7-76 Text en Copyright © 2007 Ramaswamy and Ioshikhes; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Ramaswamy, Amutha
Ioshikhes, Ilya
Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone
title Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone
title_full Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone
title_fullStr Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone
title_full_unstemmed Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone
title_short Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone
title_sort global dynamics of newly constructed oligonucleosomes of conventional and variant h2a.z histone
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2216022/
https://www.ncbi.nlm.nih.gov/pubmed/17996059
http://dx.doi.org/10.1186/1472-6807-7-76
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