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http://hdl.handle.net/2445/48184
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DC Field | Value | Language |
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dc.contributor.author | Renault, Marie | - |
dc.contributor.author | García, Jesús | - |
dc.contributor.author | Cordeiro, Tiago N. | - |
dc.contributor.author | Baldus, Marc | - |
dc.contributor.author | Pons Vallès, Miquel | - |
dc.date.accessioned | 2013-11-29T07:23:51Z | - |
dc.date.available | 2013-11-29T07:23:51Z | - |
dc.date.issued | 2013-05-13 | - |
dc.identifier.issn | 1742-464X | - |
dc.identifier.uri | http://hdl.handle.net/2445/48184 | - |
dc.description.abstract | Members of the histone-like nucleoid structuring protein (H-NS) family play roles both as architectural proteins and as modulators of gene expression in Gram-negative bacteria. The H-NS protein participates in modulatory processes that respond to environmental changes in osmolarity, pH, or temperature. H-NS oligomerization is essential for its activity. Structural models of different truncated forms are available. However, high-resolution structural details of full-length H-NS and its DNA-bound state have largely remained elusive. We report on progress in characterizing the biologically active H-NS oligomers with solid-state NMR. We compared uniformly ((13)C,(15)N)-labeled ssNMR preparations of the isolated N-terminal region (H-NS 1-47) and full-length H-NS (H-NS 1-137). In both cases, we obtained ssNMR spectra of good quality and characteristic of well-folded proteins. Analysis of the results of 2D and 3D (13)C-(13)C and (15)N-(13)C correlation experiments conducted at high magnetic field led to assignments of residues located in different topological regions of the free full-length H-NS. These findings confirm that the structure of the N-terminal dimerization domain is conserved in the oligomeric full-length protein. Small changes in the dimerization interface suggested by localized chemical shift variations between solution and solid-state spectra may be relevant for DNA recoginition. | - |
dc.format.extent | 33 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Federation of European Biochemical Societies | - |
dc.relation.isformatof | Versió preprint del document publicat a: http://dx.doi.org/10.1111/febs.12297 | - |
dc.relation.ispartof | The FEBS Journal, 2013, vol. 280, num. 12, p. 2916-2928 | - |
dc.relation.uri | http://dx.doi.org/10.1111/febs.12297 | - |
dc.rights | (c) Federation of European Biochemical Societies, 2013 | - |
dc.source | Articles publicats en revistes (Química Inorgànica i Orgànica) | - |
dc.subject.classification | Cromatina | - |
dc.subject.classification | Histones | - |
dc.subject.classification | Proteïnes | - |
dc.subject.classification | Ressonància magnètica nuclear | - |
dc.subject.classification | ADN | - |
dc.subject.classification | Ciències de la salut | - |
dc.subject.classification | Oligòmers | - |
dc.subject.other | Chromatin | - |
dc.subject.other | Histones | - |
dc.subject.other | Proteins | - |
dc.subject.other | Nuclear magnetic resonance | - |
dc.subject.other | DNA | - |
dc.subject.other | Medical sciences | - |
dc.subject.other | Oligomers | - |
dc.title | Protein oligomers studied by solid-state NMR the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/submittedVersion | - |
dc.identifier.idgrec | 629434 | - |
dc.date.updated | 2013-11-29T07:23:51Z | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/FP7/261863EU//BIO-NMR | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/FP7/211800/EU//SBMPS | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) Publicacions de projectes de recerca finançats per la UE |
Files in This Item:
File | Description | Size | Format | |
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629434.pdf | 4.6 MB | Adobe PDF | View/Open |
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