Biophysical characterization of the association of histones with single-stranded DNA

BACKGROUND: Despite the profound current knowledge of the architecture and dynamics of nucleosomes, little is known about the structures generated by the interaction of histones with single-stranded DNA (ssDNA), which is widely present during replication and transcription. METHODS: Non-denaturing ge...

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Autores: Wang, Ying, Merwyk, Luis Van, Tönsing, Katja, Walhorn, Volker, Anselmetti, Dario, Fernàndez Busquets, Xavier
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2017
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/115793
Acceso en línea:https://hdl.handle.net/2445/115793
Access Level:acceso abierto
Palabra clave:Histones
Cromatina
Chromatine
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spelling Biophysical characterization of the association of histones with single-stranded DNAWang, YingMerwyk, Luis VanTönsing, KatjaWalhorn, VolkerAnselmetti, DarioFernàndez Busquets, XavierHistonesCromatinaHistonesChromatineBACKGROUND: Despite the profound current knowledge of the architecture and dynamics of nucleosomes, little is known about the structures generated by the interaction of histones with single-stranded DNA (ssDNA), which is widely present during replication and transcription. METHODS: Non-denaturing gel electrophoresis, transmission electron microscopy, atomic force microscopy, magnetic tweezers. RESULTS: Histones have a high affinity for ssDNA at physiological salt concentrations, with an apparent binding constant similar to that calculated for their association with double-stranded DNA (dsDNA). The length of DNA (number of nucleotides in ssDNA or base pairs in dsDNA) associated with a fixed core histone mass is the same for both ssDNA and dsDNA. Whereas histone-ssDNA complexes show a high tendency to aggregate in 0.2 M NaCl, at lower ionic strength nucleosome-like structures are formed. Core histones are able to protect ssDNA from digestion by micrococcal nuclease, and a shortening of ssDNA occurs upon its interaction with histones. The purified (+) strand of a cloned DNA fragment of nucleosomal origin has a higher affinity for histones than the purified complementary (-) strand. CONCLUSIONS: At physiological ionic strength histones have high affinity for ssDNA, possibly associating with it into nucleosome-like structures. General Significance In the cell nucleus histones may spontaneously interact with ssDNA to facilitate their participation in the replication and transcription of chromatin.Elsevier2017201820172017info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersion29 p.application/pdfhttps://hdl.handle.net/2445/115793Articles publicats en revistes (ISGlobal)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésVersió postprint del document publicat a: http://dx.doi.org/10.1016/j.bbagen.2017.07.018Biochimica et Biophysica Acta. General Subjects, 2017http://dx.doi.org/10.1016/j.bbagen.2017.07.018cc-by-nc-nd (c) Elsevier, 2017http://creativecommons.org/licenses/by-nc-nd/3.0/esinfo:eu-repo/semantics/openAccessoai:recercat.cat:2445/1157932026-05-29T05:05:01Z
dc.title.none.fl_str_mv Biophysical characterization of the association of histones with single-stranded DNA
title Biophysical characterization of the association of histones with single-stranded DNA
spellingShingle Biophysical characterization of the association of histones with single-stranded DNA
Wang, Ying
Histones
Cromatina
Histones
Chromatine
title_short Biophysical characterization of the association of histones with single-stranded DNA
title_full Biophysical characterization of the association of histones with single-stranded DNA
title_fullStr Biophysical characterization of the association of histones with single-stranded DNA
title_full_unstemmed Biophysical characterization of the association of histones with single-stranded DNA
title_sort Biophysical characterization of the association of histones with single-stranded DNA
dc.creator.none.fl_str_mv Wang, Ying
Merwyk, Luis Van
Tönsing, Katja
Walhorn, Volker
Anselmetti, Dario
Fernàndez Busquets, Xavier
author Wang, Ying
author_facet Wang, Ying
Merwyk, Luis Van
Tönsing, Katja
Walhorn, Volker
Anselmetti, Dario
Fernàndez Busquets, Xavier
author_role author
author2 Merwyk, Luis Van
Tönsing, Katja
Walhorn, Volker
Anselmetti, Dario
Fernàndez Busquets, Xavier
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Histones
Cromatina
Histones
Chromatine
topic Histones
Cromatina
Histones
Chromatine
description BACKGROUND: Despite the profound current knowledge of the architecture and dynamics of nucleosomes, little is known about the structures generated by the interaction of histones with single-stranded DNA (ssDNA), which is widely present during replication and transcription. METHODS: Non-denaturing gel electrophoresis, transmission electron microscopy, atomic force microscopy, magnetic tweezers. RESULTS: Histones have a high affinity for ssDNA at physiological salt concentrations, with an apparent binding constant similar to that calculated for their association with double-stranded DNA (dsDNA). The length of DNA (number of nucleotides in ssDNA or base pairs in dsDNA) associated with a fixed core histone mass is the same for both ssDNA and dsDNA. Whereas histone-ssDNA complexes show a high tendency to aggregate in 0.2 M NaCl, at lower ionic strength nucleosome-like structures are formed. Core histones are able to protect ssDNA from digestion by micrococcal nuclease, and a shortening of ssDNA occurs upon its interaction with histones. The purified (+) strand of a cloned DNA fragment of nucleosomal origin has a higher affinity for histones than the purified complementary (-) strand. CONCLUSIONS: At physiological ionic strength histones have high affinity for ssDNA, possibly associating with it into nucleosome-like structures. General Significance In the cell nucleus histones may spontaneously interact with ssDNA to facilitate their participation in the replication and transcription of chromatin.
publishDate 2017
dc.date.none.fl_str_mv 2017
2017
2017
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/115793
url https://hdl.handle.net/2445/115793
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: http://dx.doi.org/10.1016/j.bbagen.2017.07.018
Biochimica et Biophysica Acta. General Subjects, 2017
http://dx.doi.org/10.1016/j.bbagen.2017.07.018
dc.rights.none.fl_str_mv cc-by-nc-nd (c) Elsevier, 2017
http://creativecommons.org/licenses/by-nc-nd/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc-nd (c) Elsevier, 2017
http://creativecommons.org/licenses/by-nc-nd/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 29 p.
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Articles publicats en revistes (ISGlobal)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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