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http://hdl.handle.net/2445/115793
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DC Field | Value | Language |
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dc.contributor.author | Wang, Ying | - |
dc.contributor.author | Merwyk, Luis Van | - |
dc.contributor.author | Tönsing, Katja | - |
dc.contributor.author | Walhorn, Volker | - |
dc.contributor.author | Anselmetti, Dario | - |
dc.contributor.author | Fernàndez Busquets, Xavier | - |
dc.date.accessioned | 2017-09-26T10:54:45Z | - |
dc.date.available | 2018-07-27T22:01:20Z | - |
dc.date.issued | 2017-07-27 | - |
dc.identifier.issn | 0006-3002 | - |
dc.identifier.uri | http://hdl.handle.net/2445/115793 | - |
dc.description.abstract | 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. | - |
dc.format.extent | 29 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier | - |
dc.relation.isformatof | Versió postprint del document publicat a: http://dx.doi.org/10.1016/j.bbagen.2017.07.018 | - |
dc.relation.ispartof | Biochimica et Biophysica Acta. General Subjects, 2017 | - |
dc.relation.uri | http://dx.doi.org/10.1016/j.bbagen.2017.07.018 | - |
dc.rights | cc-by-nc-nd (c) Elsevier, 2017 | - |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/es | - |
dc.source | Articles publicats en revistes (ISGlobal) | - |
dc.subject.classification | Histones | - |
dc.subject.classification | Cromatina | - |
dc.subject.other | Histones | - |
dc.subject.other | Chromatine | - |
dc.title | Biophysical characterization of the association of histones with single-stranded DNA | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/acceptedVersion | - |
dc.date.updated | 2017-08-30T18:00:31Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
Appears in Collections: | Articles publicats en revistes (ISGlobal) |
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File | Description | Size | Format | |
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wang2017_2652.pdf | 1.27 MB | Adobe PDF | View/Open |
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