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|Title:||Protein oligomers studied by solid-state NMR the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein|
Cordeiro, Tiago N.
Pons Vallès, Miquel
Ressonància magnètica nuclear
Ciències de la salut
Nuclear magnetic resonance
|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|
|Appears in Collections:||Articles publicats en revistes (Química Inorgànica i Orgànica)|
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