Please use this identifier to cite or link to this item:
https://hdl.handle.net/2445/48184
Title: | Protein oligomers studied by solid-state NMR the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein |
Author: | Renault, Marie García, Jesús Cordeiro, Tiago N. Baldus, Marc Pons Vallès, Miquel |
Keywords: | Cromatina Histones Proteïnes Ressonància magnètica nuclear ADN Ciències de la salut Oligòmers Chromatin Histones Proteins Nuclear magnetic resonance DNA Medical sciences Oligomers |
Issue Date: | 13-May-2013 |
Publisher: | Federation of European Biochemical Societies |
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. |
Note: | Versió preprint del document publicat a: http://dx.doi.org/10.1111/febs.12297 |
It is part of: | The FEBS Journal, 2013, vol. 280, num. 12, p. 2916-2928 |
URI: | https://hdl.handle.net/2445/48184 |
Related resource: | http://dx.doi.org/10.1111/febs.12297 |
ISSN: | 1742-464X |
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 | |
---|---|---|---|---|
629434.pdf | 4.6 MB | Adobe PDF | View/Open |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.