Please use this identifier to cite or link to this item: http://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
Related resource: http://dx.doi.org/10.1111/febs.12297
URI: http://hdl.handle.net/2445/48184
ISSN: 1742-464X
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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